---
_id: '7525'
abstract:
- lang: eng
text: "The medial habenula (MHb) is an evolutionary conserved epithalamic structure
important for the modulation of emotional memory. It is involved in regulation
of anxiety, compulsive behavior, addiction (nicotinic and opioid), sexual and
feeding behavior. MHb receives inputs from septal regions and projects exclusively
to the interpeduncular nucleus (IPN). Distinct sub-regions of the septum project
to different subnuclei of MHb: the bed nucleus of anterior commissure projects
to dorsal MHb and the triangular septum projects to ventral MHb. Furthermore,
the dorsal and ventral MHb project to the lateral and rostral/central IPN, respectively.
Importantly, these projections have unique features of prominent co-release of
different neurotransmitters and requirement of a peculiar type of calcium channel
for release. In general, synaptic neurotransmission requires an activity-dependent
influx of Ca2+ into the presynaptic terminal through voltage-gated calcium channels.
The calcium channel family most commonly involved in neurotransmitter release
comprises three members, P/Q-, N- and R-type with Cav2.1, Cav2.2 and Cav2.3 subunits,
respectively. In contrast to most CNS synapses that mainly express Cav2.1 and/or
Cav2.2, MHb terminals in the IPN exclusively express Cav2.3. In other parts of
the brain, such as the hippocampus, Cav2.3 is mostly located to postsynaptic elements.
This unusual presynaptic location of Cav2.3 in the MHb-IPN pathway implies unique
mechanisms of glutamate release in this pathway. One potential example of such
uniqueness is the facilitation of release by GABAB receptor (GBR) activation.
Presynaptic GBRs usually inhibit the release of neurotransmitters by inhibiting
presynaptic calcium channels. MHb shows the highest expression levels of GBR in
the brain. GBRs comprise two subunits, GABAB1 (GB1) and GABAB2 (GB2), and are
associated with auxiliary subunits, called potassium channel tetramerization domain
containing proteins (KCTD) 8, 12, 12b and 16. Among these four subunits, KCTD12b
is exclusively expressed in ventral MHb, and KCTD8 shows the strongest expression
in the whole MHb among other brain regions, indicating that KCTD8 and KCTD12b
may be involved in the unique mechanisms of neurotransmitter release mediated
by Cav2.3 and regulated by GBRs in this pathway. \r\nIn the present study, we
first verified that neurotransmission in both dorsal and ventral MHb-IPN pathways
is mainly mediated by Cav2.3 using a selective blocker of R-type channels, SNX-482.
We next found that baclofen, a GBR agonist, has facilitatory effects on release
from ventral MHb terminal in rostral IPN, whereas it has inhibitory effects on
release from dorsal MHb terminals in lateral IPN, indicating that KCTD12b expressed
exclusively in ventral MHb may have a role in the facilitatory effects of GBR
activation. In a heterologous expression system using HEK cells, we found that
KCTD8 and KCTD12b but not KCTD12 directly bind with Cav2.3. Pre-embedding immunogold
electron microscopy data show that Cav2.3 and KCTD12b are distributed most densely
in presynaptic active zone in IPN with KCTD12b being present only in rostral/central
but not lateral IPN, whereas GABAB, KCTD8 and KCTD12 are distributed most densely
in perisynaptic sites with KCTD12 present more frequently in postsynaptic elements
and only in rostral/central IPN. In freeze-fracture replica labelling, Cav2.3,
KCTD8 and KCTD12b are co-localized with each other in the same active zone indicating
that they may form complexes regulating vesicle release in rostral IPN. \r\nOn
electrophysiological studies of wild type (WT) mice, we found that paired-pulse
ratio in rostral IPN of KCTD12b knock-out (KO) mice is lower than those of WT
and KCTD8 KO mice. Consistent with this finding, in mean variance analysis, release
probability in rostral IPN of KCTD12b KO mice is higher than that of WT and KCTD8
KO mice. Although paired-pulse ratios are not different between WT and KCTD8 KO
mice, the mean variance analysis revealed significantly lower release probability
in rostral IPN of KCTD8 KO than WT mice. These results demonstrate bidirectional
regulation of Cav2.3-mediated release by KCTD8 and KCTD12b without GBR activation
in rostral IPN. Finally, we examined the baclofen effects in rostral IPN of KCTD8
and KCTD12b KO mice, and found the facilitation of release remained in both KO
mice, indicating that the peculiar effects of the GBR activation in this pathway
do not depend on the selective expression of these KCTD subunits in ventral MHb.
However, we found that presynaptic potentiation of evoked EPSC amplitude by baclofen
falls to baseline after washout faster in KCTD12b KO mice than WT, KCTD8 KO and
KCTD8/12b double KO mice. This result indicates that KCTD12b is involved in sustained
potentiation of vesicle release by GBR activation, whereas KCTD8 is involved in
its termination in the absence of KCTD12b. Consistent with these functional findings,
replica labelling revealed an increase in density of KCTD8, but not Cav2.3 or
GBR at active zone in rostral IPN of KCTD12b KO mice compared with that of WT
mice, suggesting that increased association of KCTD8 with Cav2.3 facilitates the
release probability and termination of the GBR effect in the absence of KCTD12b.\r\nIn
summary, our study provided new insights into the physiological roles of presynaptic
Cav2.3, GBRs and their auxiliary subunits KCTDs at an evolutionary conserved neuronal
circuit. Future studies will be required to identify the exact molecular mechanism
underlying the GBR-mediated presynaptic potentiation on ventral MHb terminals.
It remains to be determined whether the prominent presence of presynaptic KCTDs
at active zone could exert similar neuromodulatory functions in different pathways
of the brain.\r\n"
acknowledged_ssus:
- _id: EM-Fac
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Pradeep
full_name: Bhandari, Pradeep
id: 45EDD1BC-F248-11E8-B48F-1D18A9856A87
last_name: Bhandari
orcid: 0000-0003-0863-4481
citation:
ama: Bhandari P. Localization and functional role of Cav2.3 in the medial habenula
to interpeduncular nucleus pathway. 2020. doi:10.15479/AT:ISTA:7525
apa: Bhandari, P. (2020). Localization and functional role of Cav2.3 in the medial
habenula to interpeduncular nucleus pathway. Institute of Science and Technology
Austria. https://doi.org/10.15479/AT:ISTA:7525
chicago: Bhandari, Pradeep. “Localization and Functional Role of Cav2.3 in the Medial
Habenula to Interpeduncular Nucleus Pathway.” Institute of Science and Technology
Austria, 2020. https://doi.org/10.15479/AT:ISTA:7525.
ieee: P. Bhandari, “Localization and functional role of Cav2.3 in the medial habenula
to interpeduncular nucleus pathway,” Institute of Science and Technology Austria,
2020.
ista: Bhandari P. 2020. Localization and functional role of Cav2.3 in the medial
habenula to interpeduncular nucleus pathway. Institute of Science and Technology
Austria.
mla: Bhandari, Pradeep. Localization and Functional Role of Cav2.3 in the Medial
Habenula to Interpeduncular Nucleus Pathway. Institute of Science and Technology
Austria, 2020, doi:10.15479/AT:ISTA:7525.
short: P. Bhandari, Localization and Functional Role of Cav2.3 in the Medial Habenula
to Interpeduncular Nucleus Pathway, Institute of Science and Technology Austria,
2020.
date_created: 2020-02-26T10:56:37Z
date_published: 2020-02-28T00:00:00Z
date_updated: 2023-09-07T13:20:03Z
day: '28'
ddc:
- '570'
degree_awarded: PhD
department:
- _id: RySh
doi: 10.15479/AT:ISTA:7525
file:
- access_level: open_access
checksum: 4589234fdb12b4ad72273b311723a7b4
content_type: application/pdf
creator: pbhandari
date_created: 2020-02-28T08:37:53Z
date_updated: 2021-03-01T23:30:04Z
embargo: 2021-02-28
file_id: '7538'
file_name: Pradeep Bhandari Thesis.pdf
file_size: 9646346
relation: main_file
title: Localization and functional role of Cav2.3 in the medial habenula to interpeduncular
nucleus pathway
- access_level: closed
checksum: aa79490553ca0a5c9b6fbcd152e93928
content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: pbhandari
date_created: 2020-02-28T08:47:14Z
date_updated: 2021-03-01T23:30:04Z
embargo_to: open_access
file_id: '7539'
file_name: Pradeep Bhandari Thesis.docx
file_size: 35252164
relation: source_file
title: Localization and functional role of Cav2.3 in the medial habenula to interpeduncular
nucleus pathway
file_date_updated: 2021-03-01T23:30:04Z
has_accepted_license: '1'
keyword:
- Cav2.3
- medial habenula (MHb)
- interpeduncular nucleus (IPN)
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: '79'
publication_identifier:
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
status: public
supervisor:
- first_name: Ryuichi
full_name: Shigemoto, Ryuichi
id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
last_name: Shigemoto
orcid: 0000-0001-8761-9444
title: Localization and functional role of Cav2.3 in the medial habenula to interpeduncular
nucleus pathway
type: dissertation
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
year: '2020'
...
---
_id: '8532'
abstract:
- lang: eng
text: The molecular anatomy of synapses defines their characteristics in transmission
and plasticity. Precise measurements of the number and distribution of synaptic
proteins are important for our understanding of synapse heterogeneity within and
between brain regions. Freeze–fracture replica immunogold electron microscopy
enables us to analyze them quantitatively on a two-dimensional membrane surface.
Here, we introduce Darea software, which utilizes deep learning for analysis of
replica images and demonstrate its usefulness for quick measurements of the pre-
and postsynaptic areas, density and distribution of gold particles at synapses
in a reproducible manner. We used Darea for comparing glutamate receptor and calcium
channel distributions between hippocampal CA3-CA1 spine synapses on apical and
basal dendrites, which differ in signaling pathways involved in synaptic plasticity.
We found that apical synapses express a higher density of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic
acid (AMPA) receptors and a stronger increase of AMPA receptors with synaptic
size, while basal synapses show a larger increase in N-methyl-D-aspartate (NMDA)
receptors with size. Interestingly, AMPA and NMDA receptors are segregated within
postsynaptic sites and negatively correlated in density among both apical and
basal synapses. In the presynaptic sites, Cav2.1 voltage-gated calcium channels
show similar densities in apical and basal synapses with distributions consistent
with an exclusion zone model of calcium channel-release site topography.
acknowledgement: "This research was funded by Austrian Academy of Sciences, DOC fellowship
to D.K., European Research\r\nCouncil Advanced Grant 694539 and European Union Human
Brain Project (HBP) SGA2 785907 to R.S.\r\nWe acknowledge Elena Hollergschwandtner
for technical support."
article_number: '6737'
article_processing_charge: No
article_type: original
author:
- first_name: David
full_name: Kleindienst, David
id: 42E121A4-F248-11E8-B48F-1D18A9856A87
last_name: Kleindienst
- first_name: Jacqueline-Claire
full_name: Montanaro-Punzengruber, Jacqueline-Claire
id: 3786AB44-F248-11E8-B48F-1D18A9856A87
last_name: Montanaro-Punzengruber
- first_name: Pradeep
full_name: Bhandari, Pradeep
id: 45EDD1BC-F248-11E8-B48F-1D18A9856A87
last_name: Bhandari
orcid: 0000-0003-0863-4481
- first_name: Matthew J
full_name: Case, Matthew J
id: 44B7CA5A-F248-11E8-B48F-1D18A9856A87
last_name: Case
- first_name: Yugo
full_name: Fukazawa, Yugo
last_name: Fukazawa
- first_name: Ryuichi
full_name: Shigemoto, Ryuichi
id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
last_name: Shigemoto
orcid: 0000-0001-8761-9444
citation:
ama: Kleindienst D, Montanaro-Punzengruber J-C, Bhandari P, Case MJ, Fukazawa Y,
Shigemoto R. Deep learning-assisted high-throughput analysis of freeze-fracture
replica images applied to glutamate receptors and calcium channels at hippocampal
synapses. International Journal of Molecular Sciences. 2020;21(18). doi:10.3390/ijms21186737
apa: Kleindienst, D., Montanaro-Punzengruber, J.-C., Bhandari, P., Case, M. J.,
Fukazawa, Y., & Shigemoto, R. (2020). Deep learning-assisted high-throughput
analysis of freeze-fracture replica images applied to glutamate receptors and
calcium channels at hippocampal synapses. International Journal of Molecular
Sciences. MDPI. https://doi.org/10.3390/ijms21186737
chicago: Kleindienst, David, Jacqueline-Claire Montanaro-Punzengruber, Pradeep Bhandari,
Matthew J Case, Yugo Fukazawa, and Ryuichi Shigemoto. “Deep Learning-Assisted
High-Throughput Analysis of Freeze-Fracture Replica Images Applied to Glutamate
Receptors and Calcium Channels at Hippocampal Synapses.” International Journal
of Molecular Sciences. MDPI, 2020. https://doi.org/10.3390/ijms21186737.
ieee: D. Kleindienst, J.-C. Montanaro-Punzengruber, P. Bhandari, M. J. Case, Y.
Fukazawa, and R. Shigemoto, “Deep learning-assisted high-throughput analysis of
freeze-fracture replica images applied to glutamate receptors and calcium channels
at hippocampal synapses,” International Journal of Molecular Sciences,
vol. 21, no. 18. MDPI, 2020.
ista: Kleindienst D, Montanaro-Punzengruber J-C, Bhandari P, Case MJ, Fukazawa Y,
Shigemoto R. 2020. Deep learning-assisted high-throughput analysis of freeze-fracture
replica images applied to glutamate receptors and calcium channels at hippocampal
synapses. International Journal of Molecular Sciences. 21(18), 6737.
mla: Kleindienst, David, et al. “Deep Learning-Assisted High-Throughput Analysis
of Freeze-Fracture Replica Images Applied to Glutamate Receptors and Calcium Channels
at Hippocampal Synapses.” International Journal of Molecular Sciences,
vol. 21, no. 18, 6737, MDPI, 2020, doi:10.3390/ijms21186737.
short: D. Kleindienst, J.-C. Montanaro-Punzengruber, P. Bhandari, M.J. Case, Y.
Fukazawa, R. Shigemoto, International Journal of Molecular Sciences 21 (2020).
date_created: 2020-09-20T22:01:35Z
date_published: 2020-09-14T00:00:00Z
date_updated: 2024-03-28T23:30:31Z
day: '14'
ddc:
- '570'
department:
- _id: RySh
doi: 10.3390/ijms21186737
ec_funded: 1
external_id:
isi:
- '000579945300001'
file:
- access_level: open_access
checksum: 2e4f62f3cfe945b7391fc3070e5a289f
content_type: application/pdf
creator: dernst
date_created: 2020-09-21T14:08:58Z
date_updated: 2020-09-21T14:08:58Z
file_id: '8551'
file_name: 2020_JournMolecSciences_Kleindienst.pdf
file_size: 5748456
relation: main_file
success: 1
file_date_updated: 2020-09-21T14:08:58Z
has_accepted_license: '1'
intvolume: ' 21'
isi: 1
issue: '18'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '09'
oa: 1
oa_version: Published Version
project:
- _id: 25CA28EA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '694539'
name: 'In situ analysis of single channel subunit composition in neurons: physiological
implication in synaptic plasticity and behaviour'
- _id: 25D32BC0-B435-11E9-9278-68D0E5697425
name: Mechanism of formation and maintenance of input side-dependent asymmetry in
the hippocampus
- _id: 26436750-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '785907'
name: Human Brain Project Specific Grant Agreement 2 (HBP SGA 2)
publication: International Journal of Molecular Sciences
publication_identifier:
eissn:
- '14220067'
issn:
- '16616596'
publication_status: published
publisher: MDPI
quality_controlled: '1'
related_material:
record:
- id: '9562'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Deep learning-assisted high-throughput analysis of freeze-fracture replica
images applied to glutamate receptors and calcium channels at hippocampal synapses
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 21
year: '2020'
...
---
_id: '6659'
abstract:
- lang: eng
text: Chemical labeling of proteins with synthetic molecular probes offers the possibility
to probe the functions of proteins of interest in living cells. However, the methods
for covalently labeling targeted proteins using complementary peptide tag-probe
pairs are still limited, irrespective of the versatility of such pairs in biological
research. Herein, we report the new CysHis tag-Ni(II) probe pair for the specific
covalent labeling of proteins. A broad-range evaluation of the reactivity profiles
of the probe and the CysHis peptide tag afforded a tag-probe pair with an optimized
and high labeling selectivity and reactivity. In particular, the labeling specificity
of this pair was notably improved compared to the previously reported one. This
pair was successfully utilized for the fluorescence imaging of membrane proteins
on the surfaces of living cells, demonstrating its potential utility in biological
research.
acknowledgement: his work was supported by the Grant-in-Aid for Scientific Research
B (JSPS KAKENHI grant no. JP17H03090 to A. O.); the Scientific Research on Innovative
Areas “Chemistry for Multimolecular Crowding Biosystems” (JSPS KAKENHI grant no.
JP17H06349 to A. O.); and the European Union (European Research Council Advanced
grant no. 694539 and Human Brain Project Ref. 720270 to R. S.). A. O. acknowledges
the financial support of the Takeda Science Foundation.
article_processing_charge: No
article_type: original
author:
- first_name: Naoki
full_name: Zenmyo, Naoki
last_name: Zenmyo
- first_name: Hiroki
full_name: Tokumaru, Hiroki
last_name: Tokumaru
- first_name: Shohei
full_name: Uchinomiya, Shohei
last_name: Uchinomiya
- first_name: Hirokazu
full_name: Fuchida, Hirokazu
last_name: Fuchida
- first_name: Shigekazu
full_name: Tabata, Shigekazu
id: 4427179E-F248-11E8-B48F-1D18A9856A87
last_name: Tabata
- first_name: Itaru
full_name: Hamachi, Itaru
last_name: Hamachi
- first_name: Ryuichi
full_name: Shigemoto, Ryuichi
id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
last_name: Shigemoto
orcid: 0000-0001-8761-9444
- first_name: Akio
full_name: Ojida, Akio
last_name: Ojida
citation:
ama: Zenmyo N, Tokumaru H, Uchinomiya S, et al. Optimized reaction pair of the CysHis
tag and Ni(II)-NTA probe for highly selective chemical labeling of membrane proteins.
Bulletin of the Chemical Society of Japan. 2019;92(5):995-1000. doi:10.1246/bcsj.20190034
apa: Zenmyo, N., Tokumaru, H., Uchinomiya, S., Fuchida, H., Tabata, S., Hamachi,
I., … Ojida, A. (2019). Optimized reaction pair of the CysHis tag and Ni(II)-NTA
probe for highly selective chemical labeling of membrane proteins. Bulletin
of the Chemical Society of Japan. Bulletin of the Chemical Society of Japan.
https://doi.org/10.1246/bcsj.20190034
chicago: Zenmyo, Naoki, Hiroki Tokumaru, Shohei Uchinomiya, Hirokazu Fuchida, Shigekazu
Tabata, Itaru Hamachi, Ryuichi Shigemoto, and Akio Ojida. “Optimized Reaction
Pair of the CysHis Tag and Ni(II)-NTA Probe for Highly Selective Chemical Labeling
of Membrane Proteins.” Bulletin of the Chemical Society of Japan. Bulletin
of the Chemical Society of Japan, 2019. https://doi.org/10.1246/bcsj.20190034.
ieee: N. Zenmyo et al., “Optimized reaction pair of the CysHis tag and Ni(II)-NTA
probe for highly selective chemical labeling of membrane proteins,” Bulletin
of the Chemical Society of Japan, vol. 92, no. 5. Bulletin of the Chemical
Society of Japan, pp. 995–1000, 2019.
ista: Zenmyo N, Tokumaru H, Uchinomiya S, Fuchida H, Tabata S, Hamachi I, Shigemoto
R, Ojida A. 2019. Optimized reaction pair of the CysHis tag and Ni(II)-NTA probe
for highly selective chemical labeling of membrane proteins. Bulletin of the Chemical
Society of Japan. 92(5), 995–1000.
mla: Zenmyo, Naoki, et al. “Optimized Reaction Pair of the CysHis Tag and Ni(II)-NTA
Probe for Highly Selective Chemical Labeling of Membrane Proteins.” Bulletin
of the Chemical Society of Japan, vol. 92, no. 5, Bulletin of the Chemical
Society of Japan, 2019, pp. 995–1000, doi:10.1246/bcsj.20190034.
short: N. Zenmyo, H. Tokumaru, S. Uchinomiya, H. Fuchida, S. Tabata, I. Hamachi,
R. Shigemoto, A. Ojida, Bulletin of the Chemical Society of Japan 92 (2019) 995–1000.
date_created: 2019-07-21T21:59:16Z
date_published: 2019-05-15T00:00:00Z
date_updated: 2021-01-12T08:08:26Z
day: '15'
ddc:
- '570'
department:
- _id: RySh
doi: 10.1246/bcsj.20190034
ec_funded: 1
file:
- access_level: open_access
checksum: 186de511d6e0ca93f5d981e2443eb8cd
content_type: application/pdf
creator: dernst
date_created: 2020-10-02T08:49:58Z
date_updated: 2020-10-02T08:49:58Z
file_id: '8594'
file_name: 2019_BCSJ_Zenmyo.pdf
file_size: 2464903
relation: main_file
success: 1
file_date_updated: 2020-10-02T08:49:58Z
has_accepted_license: '1'
intvolume: ' 92'
issue: '5'
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
page: 995-1000
project:
- _id: 25CA28EA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '694539'
name: 'In situ analysis of single channel subunit composition in neurons: physiological
implication in synaptic plasticity and behaviour'
publication: Bulletin of the Chemical Society of Japan
publication_identifier:
issn:
- '00092673'
publication_status: published
publisher: Bulletin of the Chemical Society of Japan
quality_controlled: '1'
scopus_import: '1'
status: public
title: Optimized reaction pair of the CysHis tag and Ni(II)-NTA probe for highly selective
chemical labeling of membrane proteins
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 92
year: '2019'
...
---
_id: '6868'
abstract:
- lang: eng
text: "Hyperpolarization-activated cyclic-nucleotide-gated (HCN) channels control
electrical rhythmicity and excitability in the heart and brain, but the function
of HCN channels at the subcellular level in axons remains poorly understood. Here,
we show that the action potential conduction velocity in both myelinated and unmyelinated
central axons can be bidirectionally modulated by a HCN channel blocker, cyclic
adenosine monophosphate (cAMP), and neuromodulators. Recordings from mouse cerebellar
mossy fiber boutons show that HCN channels ensure reliable high-frequency firing
and are strongly modulated by cAMP (EC50 40 mM; estimated endogenous cAMP concentration
13 mM). In addition, immunogold-electron microscopy revealed HCN2 as the dominating
subunit in cerebellar mossy fibers. Computational modeling indicated that HCN2
channels control conduction velocity primarily by altering the resting membrane
potential\r\nand are associated with significant metabolic costs. These results
suggest that the cAMP-HCN pathway provides neuromodulators with an opportunity
to finely tune energy consumption and temporal delays across axons in the brain."
article_number: e42766
article_processing_charge: No
article_type: original
author:
- first_name: Niklas
full_name: Byczkowicz, Niklas
last_name: Byczkowicz
- first_name: Abdelmoneim
full_name: Eshra, Abdelmoneim
last_name: Eshra
- first_name: Jacqueline-Claire
full_name: Montanaro-Punzengruber, Jacqueline-Claire
id: 3786AB44-F248-11E8-B48F-1D18A9856A87
last_name: Montanaro-Punzengruber
- first_name: Andrea
full_name: Trevisiol, Andrea
last_name: Trevisiol
- first_name: Johannes
full_name: Hirrlinger, Johannes
last_name: Hirrlinger
- first_name: Maarten Hp
full_name: Kole, Maarten Hp
last_name: Kole
- first_name: Ryuichi
full_name: Shigemoto, Ryuichi
id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
last_name: Shigemoto
orcid: 0000-0001-8761-9444
- first_name: Stefan
full_name: Hallermann, Stefan
last_name: Hallermann
citation:
ama: Byczkowicz N, Eshra A, Montanaro-Punzengruber J-C, et al. HCN channel-mediated
neuromodulation can control action potential velocity and fidelity in central
axons. eLife. 2019;8. doi:10.7554/eLife.42766
apa: Byczkowicz, N., Eshra, A., Montanaro-Punzengruber, J.-C., Trevisiol, A., Hirrlinger,
J., Kole, M. H., … Hallermann, S. (2019). HCN channel-mediated neuromodulation
can control action potential velocity and fidelity in central axons. ELife.
eLife Sciences Publications. https://doi.org/10.7554/eLife.42766
chicago: Byczkowicz, Niklas, Abdelmoneim Eshra, Jacqueline-Claire Montanaro-Punzengruber,
Andrea Trevisiol, Johannes Hirrlinger, Maarten Hp Kole, Ryuichi Shigemoto, and
Stefan Hallermann. “HCN Channel-Mediated Neuromodulation Can Control Action Potential
Velocity and Fidelity in Central Axons.” ELife. eLife Sciences Publications,
2019. https://doi.org/10.7554/eLife.42766.
ieee: N. Byczkowicz et al., “HCN channel-mediated neuromodulation can control
action potential velocity and fidelity in central axons,” eLife, vol. 8.
eLife Sciences Publications, 2019.
ista: Byczkowicz N, Eshra A, Montanaro-Punzengruber J-C, Trevisiol A, Hirrlinger
J, Kole MH, Shigemoto R, Hallermann S. 2019. HCN channel-mediated neuromodulation
can control action potential velocity and fidelity in central axons. eLife. 8,
e42766.
mla: Byczkowicz, Niklas, et al. “HCN Channel-Mediated Neuromodulation Can Control
Action Potential Velocity and Fidelity in Central Axons.” ELife, vol. 8,
e42766, eLife Sciences Publications, 2019, doi:10.7554/eLife.42766.
short: N. Byczkowicz, A. Eshra, J.-C. Montanaro-Punzengruber, A. Trevisiol, J. Hirrlinger,
M.H. Kole, R. Shigemoto, S. Hallermann, ELife 8 (2019).
date_created: 2019-09-15T22:00:43Z
date_published: 2019-09-09T00:00:00Z
date_updated: 2023-08-30T06:17:06Z
day: '09'
ddc:
- '570'
department:
- _id: RySh
doi: 10.7554/eLife.42766
external_id:
isi:
- '000485663900001'
file:
- access_level: open_access
checksum: c350b7861ef0fb537cae8a3232aec016
content_type: application/pdf
creator: dernst
date_created: 2019-09-16T13:14:33Z
date_updated: 2020-07-14T12:47:42Z
file_id: '6880'
file_name: 2019_eLife_Byczkowicz.pdf
file_size: 4008137
relation: main_file
file_date_updated: 2020-07-14T12:47:42Z
has_accepted_license: '1'
intvolume: ' 8'
isi: 1
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
publication: eLife
publication_identifier:
eissn:
- 2050084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: HCN channel-mediated neuromodulation can control action potential velocity
and fidelity in central axons
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 8
year: '2019'
...
---
_id: '7099'
acknowledgement: "The authors thank Gabi Schmid for excellent technical support. We
also thank\r\nDr. H. Harada, Dr. W. Kaufmann, and Dr. B. Kapelari for testing the
specificity\r\nof some of the antibodies used in this study on replicas. Funding
was provided\r\nby the Austrian Science Fund (Fonds zur Fo¨ rderung der Wissenschaftlichen\r\nForschung)
Sonderforschungsbereich grants F44-17 (to F.jF.), F44-10 and\r\nP25375-B24 (to N.S.),
and P26680 (to G.S.) and by the Novartis Research\r\nFoundation and the Swiss National
Science Foundation (to A.L). We also thank\r\nProf. M. Capogna for reading a previous
version of the manuscript."
article_processing_charge: No
article_type: original
author:
- first_name: Yu
full_name: Kasugai, Yu
last_name: Kasugai
- first_name: Elisabeth
full_name: Vogel, Elisabeth
last_name: Vogel
- first_name: Heide
full_name: Hörtnagl, Heide
last_name: Hörtnagl
- first_name: Sabine
full_name: Schönherr, Sabine
last_name: Schönherr
- first_name: Enrica
full_name: Paradiso, Enrica
last_name: Paradiso
- first_name: Markus
full_name: Hauschild, Markus
last_name: Hauschild
- first_name: Georg
full_name: Göbel, Georg
last_name: Göbel
- first_name: Ivan
full_name: Milenkovic, Ivan
last_name: Milenkovic
- first_name: Yvan
full_name: Peterschmitt, Yvan
last_name: Peterschmitt
- first_name: Ramon
full_name: Tasan, Ramon
last_name: Tasan
- first_name: Günther
full_name: Sperk, Günther
last_name: Sperk
- first_name: Ryuichi
full_name: Shigemoto, Ryuichi
id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
last_name: Shigemoto
orcid: 0000-0001-8761-9444
- first_name: Werner
full_name: Sieghart, Werner
last_name: Sieghart
- first_name: Nicolas
full_name: Singewald, Nicolas
last_name: Singewald
- first_name: Andreas
full_name: Lüthi, Andreas
last_name: Lüthi
- first_name: Francesco
full_name: Ferraguti, Francesco
last_name: Ferraguti
citation:
ama: Kasugai Y, Vogel E, Hörtnagl H, et al. Structural and functional remodeling
of amygdala GABAergic synapses in associative fear learning. Neuron. 2019;104(4):781-794.e4.
doi:10.1016/j.neuron.2019.08.013
apa: Kasugai, Y., Vogel, E., Hörtnagl, H., Schönherr, S., Paradiso, E., Hauschild,
M., … Ferraguti, F. (2019). Structural and functional remodeling of amygdala GABAergic
synapses in associative fear learning. Neuron. Elsevier. https://doi.org/10.1016/j.neuron.2019.08.013
chicago: Kasugai, Yu, Elisabeth Vogel, Heide Hörtnagl, Sabine Schönherr, Enrica
Paradiso, Markus Hauschild, Georg Göbel, et al. “Structural and Functional Remodeling
of Amygdala GABAergic Synapses in Associative Fear Learning.” Neuron. Elsevier,
2019. https://doi.org/10.1016/j.neuron.2019.08.013.
ieee: Y. Kasugai et al., “Structural and functional remodeling of amygdala
GABAergic synapses in associative fear learning,” Neuron, vol. 104, no.
4. Elsevier, p. 781–794.e4, 2019.
ista: Kasugai Y, Vogel E, Hörtnagl H, Schönherr S, Paradiso E, Hauschild M, Göbel
G, Milenkovic I, Peterschmitt Y, Tasan R, Sperk G, Shigemoto R, Sieghart W, Singewald
N, Lüthi A, Ferraguti F. 2019. Structural and functional remodeling of amygdala
GABAergic synapses in associative fear learning. Neuron. 104(4), 781–794.e4.
mla: Kasugai, Yu, et al. “Structural and Functional Remodeling of Amygdala GABAergic
Synapses in Associative Fear Learning.” Neuron, vol. 104, no. 4, Elsevier,
2019, p. 781–794.e4, doi:10.1016/j.neuron.2019.08.013.
short: Y. Kasugai, E. Vogel, H. Hörtnagl, S. Schönherr, E. Paradiso, M. Hauschild,
G. Göbel, I. Milenkovic, Y. Peterschmitt, R. Tasan, G. Sperk, R. Shigemoto, W.
Sieghart, N. Singewald, A. Lüthi, F. Ferraguti, Neuron 104 (2019) 781–794.e4.
date_created: 2019-11-25T08:02:39Z
date_published: 2019-11-20T00:00:00Z
date_updated: 2023-08-30T07:28:22Z
day: '20'
ddc:
- '571'
- '599'
department:
- _id: RySh
doi: 10.1016/j.neuron.2019.08.013
external_id:
isi:
- '000497963500017'
pmid:
- '31543297'
has_accepted_license: '1'
intvolume: ' 104'
isi: 1
issue: '4'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.neuron.2019.08.013
month: '11'
oa: 1
oa_version: Published Version
page: 781-794.e4
pmid: 1
publication: Neuron
publication_identifier:
issn:
- 0896-6273
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structural and functional remodeling of amygdala GABAergic synapses in associative
fear learning
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 104
year: '2019'
...
---
_id: '7179'
abstract:
- lang: eng
text: Glutamate is the major excitatory neurotransmitter in the CNS binding to a
variety of glutamate receptors. Metabotropic glutamate receptors (mGluR1 to mGluR8)
can act excitatory or inhibitory, depending on associated signal cascades. Expression
and localization of inhibitory acting mGluRs at inner hair cells (IHCs) in the
cochlea are largely unknown. Here, we analyzed expression of mGluR2, mGluR3, mGluR4,
mGluR6, mGluR7, and mGluR8 and investigated their localization with respect to
the presynaptic ribbon of IHC synapses. We detected transcripts for mGluR2, mGluR3,
and mGluR4 as well as for mGluR7a, mGluR7b, mGluR8a, and mGluR8b splice variants.
Using receptor-specific antibodies in cochlear wholemounts, we found expression
of mGluR2, mGluR4, and mGluR8b close to presynaptic ribbons. Super resolution
and confocal microscopy in combination with 3-dimensional reconstructions indicated
a postsynaptic localization of mGluR2 that overlaps with postsynaptic density
protein 95 on dendrites of afferent type I spiral ganglion neurons. In contrast,
mGluR4 and mGluR8b were expressed at the presynapse close to IHC ribbons. In summary,
we localized in detail 3 mGluR types at IHC ribbon synapses, providing a fundament
for new therapeutical strategies that could protect the cochlea against noxious
stimuli and excitotoxicity.
article_processing_charge: No
article_type: original
author:
- first_name: Lisa
full_name: Klotz, Lisa
last_name: Klotz
- first_name: Olaf
full_name: Wendler, Olaf
last_name: Wendler
- first_name: Renato
full_name: Frischknecht, Renato
last_name: Frischknecht
- first_name: Ryuichi
full_name: Shigemoto, Ryuichi
id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
last_name: Shigemoto
orcid: 0000-0001-8761-9444
- first_name: Holger
full_name: Schulze, Holger
last_name: Schulze
- first_name: Ralf
full_name: Enz, Ralf
last_name: Enz
citation:
ama: Klotz L, Wendler O, Frischknecht R, Shigemoto R, Schulze H, Enz R. Localization
of group II and III metabotropic glutamate receptors at pre- and postsynaptic
sites of inner hair cell ribbon synapses. FASEB Journal. 2019;33(12):13734-13746.
doi:10.1096/fj.201901543R
apa: Klotz, L., Wendler, O., Frischknecht, R., Shigemoto, R., Schulze, H., &
Enz, R. (2019). Localization of group II and III metabotropic glutamate receptors
at pre- and postsynaptic sites of inner hair cell ribbon synapses. FASEB Journal.
FASEB. https://doi.org/10.1096/fj.201901543R
chicago: Klotz, Lisa, Olaf Wendler, Renato Frischknecht, Ryuichi Shigemoto, Holger
Schulze, and Ralf Enz. “Localization of Group II and III Metabotropic Glutamate
Receptors at Pre- and Postsynaptic Sites of Inner Hair Cell Ribbon Synapses.”
FASEB Journal. FASEB, 2019. https://doi.org/10.1096/fj.201901543R.
ieee: L. Klotz, O. Wendler, R. Frischknecht, R. Shigemoto, H. Schulze, and R. Enz,
“Localization of group II and III metabotropic glutamate receptors at pre- and
postsynaptic sites of inner hair cell ribbon synapses,” FASEB Journal,
vol. 33, no. 12. FASEB, pp. 13734–13746, 2019.
ista: Klotz L, Wendler O, Frischknecht R, Shigemoto R, Schulze H, Enz R. 2019. Localization
of group II and III metabotropic glutamate receptors at pre- and postsynaptic
sites of inner hair cell ribbon synapses. FASEB Journal. 33(12), 13734–13746.
mla: Klotz, Lisa, et al. “Localization of Group II and III Metabotropic Glutamate
Receptors at Pre- and Postsynaptic Sites of Inner Hair Cell Ribbon Synapses.”
FASEB Journal, vol. 33, no. 12, FASEB, 2019, pp. 13734–46, doi:10.1096/fj.201901543R.
short: L. Klotz, O. Wendler, R. Frischknecht, R. Shigemoto, H. Schulze, R. Enz,
FASEB Journal 33 (2019) 13734–13746.
date_created: 2019-12-15T23:00:42Z
date_published: 2019-12-01T00:00:00Z
date_updated: 2023-09-06T14:34:36Z
day: '01'
ddc:
- '571'
- '599'
department:
- _id: RySh
doi: 10.1096/fj.201901543R
external_id:
isi:
- '000507466100054'
pmid:
- '31585509'
file:
- access_level: open_access
checksum: 79e3b72481dc32489911121cf3b7d8d0
content_type: application/pdf
creator: shigemot
date_created: 2020-12-06T17:30:09Z
date_updated: 2020-12-06T17:30:09Z
file_id: '8922'
file_name: Klotz et al 2019 EMBO Reports.pdf
file_size: 4766789
relation: main_file
success: 1
file_date_updated: 2020-12-06T17:30:09Z
has_accepted_license: '1'
intvolume: ' 33'
isi: 1
issue: '12'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Submitted Version
page: 13734-13746
pmid: 1
publication: FASEB Journal
publication_identifier:
eissn:
- '15306860'
publication_status: published
publisher: FASEB
quality_controlled: '1'
scopus_import: '1'
status: public
title: Localization of group II and III metabotropic glutamate receptors at pre- and
postsynaptic sites of inner hair cell ribbon synapses
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 33
year: '2019'
...
---
_id: '7398'
abstract:
- lang: eng
text: 'Transporters of the solute carrier 6 (SLC6) family translocate their cognate
substrate together with Na+ and Cl−. Detailed kinetic models exist for the transporters
of GABA (GAT1/SLC6A1) and the monoamines dopamine (DAT/SLC6A3) and serotonin (SERT/SLC6A4).
Here, we posited that the transport cycle of individual SLC6 transporters reflects
the physiological requirements they operate under. We tested this hypothesis by
analyzing the transport cycle of glycine transporter 1 (GlyT1/SLC6A9) and glycine
transporter 2 (GlyT2/SLC6A5). GlyT2 is the only SLC6 family member known to translocate
glycine, Na+, and Cl− in a 1:3:1 stoichiometry. We analyzed partial reactions
in real time by electrophysiological recordings. Contrary to monoamine transporters,
both GlyTs were found to have a high transport capacity driven by rapid return
of the empty transporter after release of Cl− on the intracellular side. Rapid
cycling of both GlyTs was further supported by highly cooperative binding of cosubstrate
ions and substrate such that their forward transport mode was maintained even
under conditions of elevated intracellular Na+ or Cl−. The most important differences
in the transport cycle of GlyT1 and GlyT2 arose from the kinetics of charge movement
and the resulting voltage-dependent rate-limiting reactions: the kinetics of GlyT1
were governed by transition of the substrate-bound transporter from outward- to
inward-facing conformations, whereas the kinetics of GlyT2 were governed by Na+
binding (or a related conformational change). Kinetic modeling showed that the
kinetics of GlyT1 are ideally suited for supplying the extracellular glycine levels
required for NMDA receptor activation.'
article_processing_charge: No
article_type: original
author:
- first_name: Fatma Asli
full_name: Erdem, Fatma Asli
last_name: Erdem
- first_name: Marija
full_name: Ilic, Marija
last_name: Ilic
- first_name: Peter
full_name: Koppensteiner, Peter
id: 3B8B25A8-F248-11E8-B48F-1D18A9856A87
last_name: Koppensteiner
orcid: 0000-0002-3509-1948
- first_name: Jakub
full_name: Gołacki, Jakub
last_name: Gołacki
- first_name: Gert
full_name: Lubec, Gert
last_name: Lubec
- first_name: Michael
full_name: Freissmuth, Michael
last_name: Freissmuth
- first_name: Walter
full_name: Sandtner, Walter
last_name: Sandtner
citation:
ama: Erdem FA, Ilic M, Koppensteiner P, et al. A comparison of the transport kinetics
of glycine transporter 1 and glycine transporter 2. The Journal of General
Physiology. 2019;151(8):1035-1050. doi:10.1085/jgp.201912318
apa: Erdem, F. A., Ilic, M., Koppensteiner, P., Gołacki, J., Lubec, G., Freissmuth,
M., & Sandtner, W. (2019). A comparison of the transport kinetics of glycine
transporter 1 and glycine transporter 2. The Journal of General Physiology.
Rockefeller University Press. https://doi.org/10.1085/jgp.201912318
chicago: Erdem, Fatma Asli, Marija Ilic, Peter Koppensteiner, Jakub Gołacki, Gert
Lubec, Michael Freissmuth, and Walter Sandtner. “A Comparison of the Transport
Kinetics of Glycine Transporter 1 and Glycine Transporter 2.” The Journal of
General Physiology. Rockefeller University Press, 2019. https://doi.org/10.1085/jgp.201912318.
ieee: F. A. Erdem et al., “A comparison of the transport kinetics of glycine
transporter 1 and glycine transporter 2,” The Journal of General Physiology,
vol. 151, no. 8. Rockefeller University Press, pp. 1035–1050, 2019.
ista: Erdem FA, Ilic M, Koppensteiner P, Gołacki J, Lubec G, Freissmuth M, Sandtner
W. 2019. A comparison of the transport kinetics of glycine transporter 1 and glycine
transporter 2. The Journal of General Physiology. 151(8), 1035–1050.
mla: Erdem, Fatma Asli, et al. “A Comparison of the Transport Kinetics of Glycine
Transporter 1 and Glycine Transporter 2.” The Journal of General Physiology,
vol. 151, no. 8, Rockefeller University Press, 2019, pp. 1035–50, doi:10.1085/jgp.201912318.
short: F.A. Erdem, M. Ilic, P. Koppensteiner, J. Gołacki, G. Lubec, M. Freissmuth,
W. Sandtner, The Journal of General Physiology 151 (2019) 1035–1050.
date_created: 2020-01-29T16:06:29Z
date_published: 2019-07-03T00:00:00Z
date_updated: 2023-09-07T14:52:23Z
day: '03'
ddc:
- '570'
department:
- _id: RySh
doi: 10.1085/jgp.201912318
external_id:
isi:
- '000478792500008'
pmid:
- '31270129'
file:
- access_level: open_access
checksum: 5706b4ccd74ee3e50bf7ecb2a203df71
content_type: application/pdf
creator: dernst
date_created: 2020-02-05T07:20:32Z
date_updated: 2020-07-14T12:47:57Z
file_id: '7450'
file_name: 2019_JGP_Erdem.pdf
file_size: 2641297
relation: main_file
file_date_updated: 2020-07-14T12:47:57Z
has_accepted_license: '1'
intvolume: ' 151'
isi: 1
issue: '8'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-sa/4.0/
month: '07'
oa: 1
oa_version: Published Version
page: 1035-1050
pmid: 1
publication: The Journal of General Physiology
publication_identifier:
eissn:
- 1540-7748
issn:
- 0022-1295
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: A comparison of the transport kinetics of glycine transporter 1 and glycine
transporter 2
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 151
year: '2019'
...
---
_id: '7391'
abstract:
- lang: eng
text: Electron microscopy (EM) is a technology that enables visualization of single
proteins at a nanometer resolution. However, current protein analysis by EM mainly
relies on immunolabeling with gold-particle-conjugated antibodies, which is compromised
by large size of antibody, precluding precise detection of protein location in
biological samples. Here, we develop a specific chemical labeling method for EM
detection of proteins at single-molecular level. Rational design of α-helical
peptide tag and probe structure provided a complementary reaction pair that enabled
specific cysteine conjugation of the tag. The developed chemical labeling with
gold-nanoparticle-conjugated probe showed significantly higher labeling efficiency
and detectability of high-density clusters of tag-fused G protein-coupled receptors
in freeze-fracture replicas compared with immunogold labeling. Furthermore, in
ultrathin sections, the spatial resolution of the chemical labeling was significantly
higher than that of antibody-mediated labeling. These results demonstrate substantial
advantages of the chemical labeling approach for single protein visualization
by EM.
article_processing_charge: No
article_type: original
author:
- first_name: Shigekazu
full_name: Tabata, Shigekazu
id: 4427179E-F248-11E8-B48F-1D18A9856A87
last_name: Tabata
- first_name: Marijo
full_name: Jevtic, Marijo
id: 4BE3BC94-F248-11E8-B48F-1D18A9856A87
last_name: Jevtic
- first_name: Nobutaka
full_name: Kurashige, Nobutaka
last_name: Kurashige
- first_name: Hirokazu
full_name: Fuchida, Hirokazu
last_name: Fuchida
- first_name: Munetsugu
full_name: Kido, Munetsugu
last_name: Kido
- first_name: Kazushi
full_name: Tani, Kazushi
last_name: Tani
- first_name: Naoki
full_name: Zenmyo, Naoki
last_name: Zenmyo
- first_name: Shohei
full_name: Uchinomiya, Shohei
last_name: Uchinomiya
- first_name: Harumi
full_name: Harada, Harumi
id: 2E55CDF2-F248-11E8-B48F-1D18A9856A87
last_name: Harada
orcid: 0000-0001-7429-7896
- first_name: Makoto
full_name: Itakura, Makoto
last_name: Itakura
- first_name: Itaru
full_name: Hamachi, Itaru
last_name: Hamachi
- first_name: Ryuichi
full_name: Shigemoto, Ryuichi
id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
last_name: Shigemoto
orcid: 0000-0001-8761-9444
- first_name: Akio
full_name: Ojida, Akio
last_name: Ojida
citation:
ama: Tabata S, Jevtic M, Kurashige N, et al. Electron microscopic detection of single
membrane proteins by a specific chemical labeling. iScience. 2019;22(12):256-268.
doi:10.1016/j.isci.2019.11.025
apa: Tabata, S., Jevtic, M., Kurashige, N., Fuchida, H., Kido, M., Tani, K., … Ojida,
A. (2019). Electron microscopic detection of single membrane proteins by a specific
chemical labeling. IScience. Elsevier. https://doi.org/10.1016/j.isci.2019.11.025
chicago: Tabata, Shigekazu, Marijo Jevtic, Nobutaka Kurashige, Hirokazu Fuchida,
Munetsugu Kido, Kazushi Tani, Naoki Zenmyo, et al. “Electron Microscopic Detection
of Single Membrane Proteins by a Specific Chemical Labeling.” IScience.
Elsevier, 2019. https://doi.org/10.1016/j.isci.2019.11.025.
ieee: S. Tabata et al., “Electron microscopic detection of single membrane
proteins by a specific chemical labeling,” iScience, vol. 22, no. 12. Elsevier,
pp. 256–268, 2019.
ista: Tabata S, Jevtic M, Kurashige N, Fuchida H, Kido M, Tani K, Zenmyo N, Uchinomiya
S, Harada H, Itakura M, Hamachi I, Shigemoto R, Ojida A. 2019. Electron microscopic
detection of single membrane proteins by a specific chemical labeling. iScience.
22(12), 256–268.
mla: Tabata, Shigekazu, et al. “Electron Microscopic Detection of Single Membrane
Proteins by a Specific Chemical Labeling.” IScience, vol. 22, no. 12, Elsevier,
2019, pp. 256–68, doi:10.1016/j.isci.2019.11.025.
short: S. Tabata, M. Jevtic, N. Kurashige, H. Fuchida, M. Kido, K. Tani, N. Zenmyo,
S. Uchinomiya, H. Harada, M. Itakura, I. Hamachi, R. Shigemoto, A. Ojida, IScience
22 (2019) 256–268.
date_created: 2020-01-29T15:56:56Z
date_published: 2019-12-20T00:00:00Z
date_updated: 2024-03-28T23:30:12Z
day: '20'
ddc:
- '570'
department:
- _id: RySh
doi: 10.1016/j.isci.2019.11.025
ec_funded: 1
external_id:
isi:
- :000504652000020
pmid:
- '31786521'
file:
- access_level: open_access
checksum: f3e90056a49f09b205b1c4f8c739ffd1
content_type: application/pdf
creator: dernst
date_created: 2020-02-04T10:48:36Z
date_updated: 2020-07-14T12:47:57Z
file_id: '7448'
file_name: 2019_iScience_Tabata.pdf
file_size: 7197776
relation: main_file
file_date_updated: 2020-07-14T12:47:57Z
has_accepted_license: '1'
intvolume: ' 22'
issue: '12'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
page: 256-268
pmid: 1
project:
- _id: 25CA28EA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '694539'
name: 'In situ analysis of single channel subunit composition in neurons: physiological
implication in synaptic plasticity and behaviour'
- _id: 25CBA828-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '720270'
name: Human Brain Project Specific Grant Agreement 1 (HBP SGA 1)
publication: iScience
publication_identifier:
issn:
- 2589-0042
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
record:
- id: '11393'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Electron microscopic detection of single membrane proteins by a specific chemical
labeling
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 22
year: '2019'
...
---
_id: '562'
abstract:
- lang: eng
text: Primary neuronal cell culture preparations are widely used to investigate
synaptic functions. This chapter describes a detailed protocol for the preparation
of a neuronal cell culture in which giant calyx-type synaptic terminals are formed.
This chapter also presents detailed protocols for utilizing the main technical
advantages provided by such a preparation, namely, labeling and imaging of synaptic
organelles and electrophysiological recordings directly from presynaptic terminals.
alternative_title:
- Methods in Molecular Biology
article_processing_charge: No
author:
- first_name: Dimitar
full_name: Dimitrov, Dimitar
last_name: Dimitrov
- first_name: Laurent
full_name: Guillaud, Laurent
last_name: Guillaud
- first_name: Kohgaku
full_name: Eguchi, Kohgaku
id: 2B7846DC-F248-11E8-B48F-1D18A9856A87
last_name: Eguchi
orcid: 0000-0002-6170-2546
- first_name: Tomoyuki
full_name: Takahashi, Tomoyuki
last_name: Takahashi
citation:
ama: 'Dimitrov D, Guillaud L, Eguchi K, Takahashi T. Culture of mouse giant central
nervous system synapses and application for imaging and electrophysiological analyses.
In: Skaper SD, ed. Neurotrophic Factors. Vol 1727. Springer; 2018:201-215.
doi:10.1007/978-1-4939-7571-6_15'
apa: Dimitrov, D., Guillaud, L., Eguchi, K., & Takahashi, T. (2018). Culture
of mouse giant central nervous system synapses and application for imaging and
electrophysiological analyses. In S. D. Skaper (Ed.), Neurotrophic Factors
(Vol. 1727, pp. 201–215). Springer. https://doi.org/10.1007/978-1-4939-7571-6_15
chicago: Dimitrov, Dimitar, Laurent Guillaud, Kohgaku Eguchi, and Tomoyuki Takahashi.
“Culture of Mouse Giant Central Nervous System Synapses and Application for Imaging
and Electrophysiological Analyses.” In Neurotrophic Factors, edited by
Stephen D. Skaper, 1727:201–15. Springer, 2018. https://doi.org/10.1007/978-1-4939-7571-6_15.
ieee: D. Dimitrov, L. Guillaud, K. Eguchi, and T. Takahashi, “Culture of mouse giant
central nervous system synapses and application for imaging and electrophysiological
analyses,” in Neurotrophic Factors, vol. 1727, S. D. Skaper, Ed. Springer,
2018, pp. 201–215.
ista: 'Dimitrov D, Guillaud L, Eguchi K, Takahashi T. 2018.Culture of mouse giant
central nervous system synapses and application for imaging and electrophysiological
analyses. In: Neurotrophic Factors. Methods in Molecular Biology, vol. 1727, 201–215.'
mla: Dimitrov, Dimitar, et al. “Culture of Mouse Giant Central Nervous System Synapses
and Application for Imaging and Electrophysiological Analyses.” Neurotrophic
Factors, edited by Stephen D. Skaper, vol. 1727, Springer, 2018, pp. 201–15,
doi:10.1007/978-1-4939-7571-6_15.
short: D. Dimitrov, L. Guillaud, K. Eguchi, T. Takahashi, in:, S.D. Skaper (Ed.),
Neurotrophic Factors, Springer, 2018, pp. 201–215.
date_created: 2018-12-11T11:47:11Z
date_published: 2018-01-01T00:00:00Z
date_updated: 2021-01-12T08:03:05Z
day: '01'
ddc:
- '570'
department:
- _id: RySh
doi: 10.1007/978-1-4939-7571-6_15
editor:
- first_name: Stephen D.
full_name: Skaper, Stephen D.
last_name: Skaper
external_id:
pmid:
- '29222783'
file:
- access_level: open_access
checksum: 8aa174ca65a56fbb19e9f88cff3ac3fd
content_type: application/pdf
creator: dernst
date_created: 2019-11-19T07:47:43Z
date_updated: 2020-07-14T12:47:09Z
file_id: '7046'
file_name: 2018_NeurotrophicFactors_Dimitrov.pdf
file_size: 787407
relation: main_file
file_date_updated: 2020-07-14T12:47:09Z
has_accepted_license: '1'
intvolume: ' 1727'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Submitted Version
page: 201 - 215
pmid: 1
publication: Neurotrophic Factors
publication_status: published
publisher: Springer
publist_id: '7252'
quality_controlled: '1'
scopus_import: 1
status: public
title: Culture of mouse giant central nervous system synapses and application for
imaging and electrophysiological analyses
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 1727
year: '2018'
...
---
_id: '41'
abstract:
- lang: eng
text: 'The small-conductance, Ca2+-activated K+ (SK) channel subtype SK2 regulates
the spike rate and firing frequency, as well as Ca2+ transients in Purkinje cells
(PCs). To understand the molecular basis by which SK2 channels mediate these functions,
we analyzed the exact location and densities of SK2 channels along the neuronal
surface of the mouse cerebellar PCs using SDS-digested freeze-fracture replica
labeling (SDS-FRL) of high sensitivity combined with quantitative analyses. Immunogold
particles for SK2 were observed on post- and pre-synaptic compartments showing
both scattered and clustered distribution patterns. We found an axo-somato-dendritic
gradient of the SK2 particle density increasing 12-fold from soma to dendritic
spines. Using two different immunogold approaches, we also found that SK2 immunoparticles
were frequently adjacent to, but never overlap with, the postsynaptic density
of excitatory synapses in PC spines. Co-immunoprecipitation analysis demonstrated
that SK2 channels form macromolecular complexes with two types of proteins that
mobilize Ca2+: CaV2.1 channels and mGlu1α receptors in the cerebellum. Freeze-fracture
replica double-labeling showed significant co-clustering of particles for SK2
with those for CaV2.1 channels and mGlu1α receptors. SK2 channels were also detected
at presynaptic sites, mostly at the presynaptic active zone (AZ), where they are
close to CaV2.1 channels, though they are not significantly co-clustered. These
data demonstrate that SK2 channels located in different neuronal compartments
can associate with distinct proteins mobilizing Ca2+, and suggest that the ultrastructural
association of SK2 with CaV2.1 and mGlu1α provides the mechanism that ensures
voltage (excitability) regulation by distinct intracellular Ca2+ transients in
PCs.'
article_number: '311'
article_processing_charge: No
article_type: original
author:
- first_name: Rafæl
full_name: Luján, Rafæl
last_name: Luján
- first_name: Carolina
full_name: Aguado, Carolina
last_name: Aguado
- first_name: Francisco
full_name: Ciruela, Francisco
last_name: Ciruela
- first_name: Xavier
full_name: Arus, Xavier
last_name: Arus
- first_name: Alejandro
full_name: Martín Belmonte, Alejandro
last_name: Martín Belmonte
- first_name: Rocío
full_name: Alfaro Ruiz, Rocío
last_name: Alfaro Ruiz
- first_name: Jesus
full_name: Martinez Gomez, Jesus
last_name: Martinez Gomez
- first_name: Luis
full_name: De La Ossa, Luis
last_name: De La Ossa
- first_name: Masahiko
full_name: Watanabe, Masahiko
last_name: Watanabe
- first_name: John
full_name: Adelman, John
last_name: Adelman
- first_name: Ryuichi
full_name: Shigemoto, Ryuichi
id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
last_name: Shigemoto
orcid: 0000-0001-8761-9444
- first_name: Yugo
full_name: Fukazawa, Yugo
last_name: Fukazawa
citation:
ama: Luján R, Aguado C, Ciruela F, et al. Sk2 channels associate with mGlu1α receptors
and CaV2.1 channels in Purkinje cells. Frontiers in Cellular Neuroscience.
2018;12. doi:10.3389/fncel.2018.00311
apa: Luján, R., Aguado, C., Ciruela, F., Arus, X., Martín Belmonte, A., Alfaro Ruiz,
R., … Fukazawa, Y. (2018). Sk2 channels associate with mGlu1α receptors and CaV2.1
channels in Purkinje cells. Frontiers in Cellular Neuroscience. Frontiers
Media. https://doi.org/10.3389/fncel.2018.00311
chicago: Luján, Rafæl, Carolina Aguado, Francisco Ciruela, Xavier Arus, Alejandro
Martín Belmonte, Rocío Alfaro Ruiz, Jesus Martinez Gomez, et al. “Sk2 Channels
Associate with MGlu1α Receptors and CaV2.1 Channels in Purkinje Cells.” Frontiers
in Cellular Neuroscience. Frontiers Media, 2018. https://doi.org/10.3389/fncel.2018.00311.
ieee: R. Luján et al., “Sk2 channels associate with mGlu1α receptors and
CaV2.1 channels in Purkinje cells,” Frontiers in Cellular Neuroscience,
vol. 12. Frontiers Media, 2018.
ista: Luján R, Aguado C, Ciruela F, Arus X, Martín Belmonte A, Alfaro Ruiz R, Martinez
Gomez J, De La Ossa L, Watanabe M, Adelman J, Shigemoto R, Fukazawa Y. 2018. Sk2
channels associate with mGlu1α receptors and CaV2.1 channels in Purkinje cells.
Frontiers in Cellular Neuroscience. 12, 311.
mla: Luján, Rafæl, et al. “Sk2 Channels Associate with MGlu1α Receptors and CaV2.1
Channels in Purkinje Cells.” Frontiers in Cellular Neuroscience, vol. 12,
311, Frontiers Media, 2018, doi:10.3389/fncel.2018.00311.
short: R. Luján, C. Aguado, F. Ciruela, X. Arus, A. Martín Belmonte, R. Alfaro Ruiz,
J. Martinez Gomez, L. De La Ossa, M. Watanabe, J. Adelman, R. Shigemoto, Y. Fukazawa,
Frontiers in Cellular Neuroscience 12 (2018).
date_created: 2018-12-11T11:44:19Z
date_published: 2018-09-19T00:00:00Z
date_updated: 2023-09-18T09:31:18Z
day: '19'
ddc:
- '570'
department:
- _id: RySh
doi: 10.3389/fncel.2018.00311
ec_funded: 1
external_id:
isi:
- '000445090100002'
file:
- access_level: open_access
checksum: 0bcaec8d596162af0b7fe3f31325d480
content_type: application/pdf
creator: dernst
date_created: 2018-12-17T08:49:03Z
date_updated: 2020-07-14T12:46:23Z
file_id: '5684'
file_name: fncel-12-00311.pdf
file_size: 6834251
relation: main_file
file_date_updated: 2020-07-14T12:46:23Z
has_accepted_license: '1'
intvolume: ' 12'
isi: 1
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
project:
- _id: 25CBA828-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '720270'
name: Human Brain Project Specific Grant Agreement 1 (HBP SGA 1)
publication: Frontiers in Cellular Neuroscience
publication_identifier:
issn:
- '16625102'
publication_status: published
publisher: Frontiers Media
publist_id: '8013'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Sk2 channels associate with mGlu1α receptors and CaV2.1 channels in Purkinje
cells
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 12
year: '2018'
...