---
_id: '9048'
abstract:
- lang: eng
text: The analogy between an equilibrium partition function and the return probability
in many-body unitary dynamics has led to the concept of dynamical quantum phase
transition (DQPT). DQPTs are defined by nonanalyticities in the return amplitude
and are present in many models. In some cases, DQPTs can be related to equilibrium
concepts, such as order parameters, yet their universal description is an open
question. In this Letter, we provide first steps toward a classification of DQPTs
by using a matrix product state description of unitary dynamics in the thermodynamic
limit. This allows us to distinguish the two limiting cases of “precession” and
“entanglement” DQPTs, which are illustrated using an analytical description in
the quantum Ising model. While precession DQPTs are characterized by a large entanglement
gap and are semiclassical in their nature, entanglement DQPTs occur near avoided
crossings in the entanglement spectrum and can be distinguished by a complex pattern
of nonlocal correlations. We demonstrate the existence of precession and entanglement
DQPTs beyond Ising models, discuss observables that can distinguish them, and
relate their interplay to complex DQPT phenomenology.
acknowledgement: "S. D. N. acknowledges funding from the Institute of Science and
Technology (IST) Austria and from the European Union’s Horizon 2020 Research and
Innovation Programme under the Marie Skłodowska-Curie Grant Agreement No. 754411.
A. M. and M. S. were supported by the European Research Council (ERC) under the
European Union’s Horizon 2020 Research and\r\nInnovation Programme (Grant Agreement
No. 850899)."
article_number: '040602'
article_processing_charge: Yes
article_type: original
author:
- first_name: Stefano
full_name: De Nicola, Stefano
id: 42832B76-F248-11E8-B48F-1D18A9856A87
last_name: De Nicola
orcid: 0000-0002-4842-6671
- first_name: Alexios
full_name: Michailidis, Alexios
id: 36EBAD38-F248-11E8-B48F-1D18A9856A87
last_name: Michailidis
orcid: 0000-0002-8443-1064
- first_name: Maksym
full_name: Serbyn, Maksym
id: 47809E7E-F248-11E8-B48F-1D18A9856A87
last_name: Serbyn
orcid: 0000-0002-2399-5827
citation:
ama: De Nicola S, Michailidis A, Serbyn M. Entanglement view of dynamical quantum
phase transitions. Physical Review Letters. 2021;126(4). doi:10.1103/physrevlett.126.040602
apa: De Nicola, S., Michailidis, A., & Serbyn, M. (2021). Entanglement view
of dynamical quantum phase transitions. Physical Review Letters. American
Physical Society. https://doi.org/10.1103/physrevlett.126.040602
chicago: De Nicola, Stefano, Alexios Michailidis, and Maksym Serbyn. “Entanglement
View of Dynamical Quantum Phase Transitions.” Physical Review Letters.
American Physical Society, 2021. https://doi.org/10.1103/physrevlett.126.040602.
ieee: S. De Nicola, A. Michailidis, and M. Serbyn, “Entanglement view of dynamical
quantum phase transitions,” Physical Review Letters, vol. 126, no. 4. American
Physical Society, 2021.
ista: De Nicola S, Michailidis A, Serbyn M. 2021. Entanglement view of dynamical
quantum phase transitions. Physical Review Letters. 126(4), 040602.
mla: De Nicola, Stefano, et al. “Entanglement View of Dynamical Quantum Phase Transitions.”
Physical Review Letters, vol. 126, no. 4, 040602, American Physical Society,
2021, doi:10.1103/physrevlett.126.040602.
short: S. De Nicola, A. Michailidis, M. Serbyn, Physical Review Letters 126 (2021).
date_created: 2021-02-01T09:20:00Z
date_published: 2021-01-29T00:00:00Z
date_updated: 2023-09-05T12:08:58Z
day: '29'
ddc:
- '530'
department:
- _id: MaSe
doi: 10.1103/physrevlett.126.040602
ec_funded: 1
external_id:
arxiv:
- '2008.04894'
isi:
- '000613148200001'
file:
- access_level: open_access
checksum: d9acbc502390ed7a97e631d23ae19ecd
content_type: application/pdf
creator: dernst
date_created: 2021-02-03T12:47:04Z
date_updated: 2021-02-03T12:47:04Z
file_id: '9074'
file_name: 2021_PhysicalRevLett_DeNicola.pdf
file_size: 398075
relation: main_file
success: 1
file_date_updated: 2021-02-03T12:47:04Z
has_accepted_license: '1'
intvolume: ' 126'
isi: 1
issue: '4'
keyword:
- General Physics and Astronomy
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
project:
- _id: 260C2330-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '754411'
name: ISTplus - Postdoctoral Fellowships
- _id: 23841C26-32DE-11EA-91FC-C7463DDC885E
call_identifier: H2020
grant_number: '850899'
name: 'Non-Ergodic Quantum Matter: Universality, Dynamics and Control'
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
status: public
title: Entanglement view of dynamical quantum phase transitions
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: 126
year: '2021'
...
---
_id: '9368'
abstract:
- lang: eng
text: The quality control system for messenger RNA (mRNA) is fundamental for cellular
activities in eukaryotes. To elucidate the molecular mechanism of 3'-Phosphoinositide-Dependent
Protein Kinase1 (PDK1), a master regulator that is essential throughout eukaryotic
growth and development, we employed a forward genetic approach to screen for suppressors
of the loss-of-function T-DNA insertion double mutant pdk1.1 pdk1.2 in Arabidopsis
thaliana. Notably, the severe growth attenuation of pdk1.1 pdk1.2 was rescued
by sop21 (suppressor of pdk1.1 pdk1.2), which harbours a loss-of-function mutation
in PELOTA1 (PEL1). PEL1 is a homologue of mammalian PELOTA and yeast (Saccharomyces
cerevisiae) DOM34p, which each form a heterodimeric complex with the GTPase HBS1
(HSP70 SUBFAMILY B SUPPRESSOR1, also called SUPERKILLER PROTEIN7, SKI7), a protein
that is responsible for ribosomal rescue and thereby assures the quality and fidelity
of mRNA molecules during translation. Genetic analysis further revealed that a
dysfunctional PEL1-HBS1 complex failed to degrade the T-DNA-disrupted PDK1 transcripts,
which were truncated but functional, and thus rescued the growth and developmental
defects of pdk1.1 pdk1.2. Our studies demonstrated the functionality of a homologous
PELOTA-HBS1 complex and identified its essential regulatory role in plants, providing
insights into the mechanism of mRNA quality control.
acknowledgement: 'We gratefully acknowledge the Arabidopsis Biological Resource Centre
(ABRC) for providing T-DNA insertional mutants, and Prof. Remko Offringa for sharing
published seeds. We thank Yuchuan Liu (Shanghai OE Biotech Co., Ltd) for help with
proteomics data analysis, Xixi Zhang (IST Austria) for providing the pDONR-P4P1r-mCherry
plasmid, and Yao Xiao (Technical University of Munich), Alexander Johnson (IST Austria)
and Hana Semeradova (IST Austria) for helpful discussions. The study was supported
by National Natural Science Foundation of China (NSFC, 31721001, 91954206, to H.-W.
X.), “Ten-Thousand Talent Program” (to H.-W. X.) and Collaborative Innovation Center
of Crop Stress Biology, Henan Province, and Austrian Science Fund (FWF): I 3630-B25
(to J. F.). S.T. was funded by a European Molecular Biology Organization (EMBO)
long-term postdoctoral fellowship (ALTF 723-2015).'
article_processing_charge: No
article_type: original
author:
- first_name: W
full_name: Kong, W
last_name: Kong
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Q
full_name: Zhao, Q
last_name: Zhao
- first_name: DL
full_name: Lin, DL
last_name: Lin
- first_name: ZH
full_name: Xu, ZH
last_name: Xu
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: HW
full_name: Xue, HW
last_name: Xue
citation:
ama: Kong W, Tan S, Zhao Q, et al. mRNA surveillance complex PELOTA-HBS1 eegulates
phosphoinositide-sependent protein kinase1 and plant growth. Plant Physiology.
2021;186(4):2003-2020. doi:10.1093/plphys/kiab199
apa: Kong, W., Tan, S., Zhao, Q., Lin, D., Xu, Z., Friml, J., & Xue, H. (2021).
mRNA surveillance complex PELOTA-HBS1 eegulates phosphoinositide-sependent protein
kinase1 and plant growth. Plant Physiology. American Society of Plant Biologists.
https://doi.org/10.1093/plphys/kiab199
chicago: Kong, W, Shutang Tan, Q Zhao, DL Lin, ZH Xu, Jiří Friml, and HW Xue. “MRNA
Surveillance Complex PELOTA-HBS1 Eegulates Phosphoinositide-Sependent Protein
Kinase1 and Plant Growth.” Plant Physiology. American Society of Plant
Biologists, 2021. https://doi.org/10.1093/plphys/kiab199.
ieee: W. Kong et al., “mRNA surveillance complex PELOTA-HBS1 eegulates phosphoinositide-sependent
protein kinase1 and plant growth,” Plant Physiology, vol. 186, no. 4. American
Society of Plant Biologists, pp. 2003–2020, 2021.
ista: Kong W, Tan S, Zhao Q, Lin D, Xu Z, Friml J, Xue H. 2021. mRNA surveillance
complex PELOTA-HBS1 eegulates phosphoinositide-sependent protein kinase1 and plant
growth. Plant Physiology. 186(4), 2003–2020.
mla: Kong, W., et al. “MRNA Surveillance Complex PELOTA-HBS1 Eegulates Phosphoinositide-Sependent
Protein Kinase1 and Plant Growth.” Plant Physiology, vol. 186, no. 4, American
Society of Plant Biologists, 2021, pp. 2003–20, doi:10.1093/plphys/kiab199.
short: W. Kong, S. Tan, Q. Zhao, D. Lin, Z. Xu, J. Friml, H. Xue, Plant Physiology
186 (2021) 2003–2020.
date_created: 2021-05-03T13:28:20Z
date_published: 2021-04-30T00:00:00Z
date_updated: 2023-09-05T12:20:27Z
day: '30'
department:
- _id: JiFr
doi: 10.1093/plphys/kiab199
external_id:
isi:
- '000703922000025'
pmid:
- '33930167'
intvolume: ' 186'
isi: 1
issue: '4'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1093/plphys/kiab199
month: '04'
oa: 1
oa_version: Published Version
page: 2003-2020
pmid: 1
project:
- _id: 256FEF10-B435-11E9-9278-68D0E5697425
grant_number: 723-2015
name: Long Term Fellowship
- _id: 26538374-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I03630
name: Molecular mechanisms of endocytic cargo recognition in plants
publication: Plant Physiology
publication_identifier:
eissn:
- 1532-2548
issn:
- 0032-0889
publication_status: published
publisher: American Society of Plant Biologists
quality_controlled: '1'
status: public
title: mRNA surveillance complex PELOTA-HBS1 eegulates phosphoinositide-sependent
protein kinase1 and plant growth
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 186
year: '2021'
...
---
_id: '10860'
abstract:
- lang: eng
text: A tight frame is the orthogonal projection of some orthonormal basis of Rn
onto Rk. We show that a set of vectors is a tight frame if and only if the set
of all cross products of these vectors is a tight frame. We reformulate a range
of problems on the volume of projections (or sections) of regular polytopes in
terms of tight frames and write a first-order necessary condition for local extrema
of these problems. As applications, we prove new results for the problem of maximization
of the volume of zonotopes.
acknowledgement: The author was supported by the Swiss National Science Foundation
grant 200021_179133. The author acknowledges the financial support from the Ministry
of Education and Science of the Russian Federation in the framework of MegaGrant
no. 075-15-2019-1926.
article_processing_charge: No
article_type: original
author:
- first_name: Grigory
full_name: Ivanov, Grigory
id: 87744F66-5C6F-11EA-AFE0-D16B3DDC885E
last_name: Ivanov
citation:
ama: Ivanov G. Tight frames and related geometric problems. Canadian Mathematical
Bulletin. 2021;64(4):942-963. doi:10.4153/s000843952000096x
apa: Ivanov, G. (2021). Tight frames and related geometric problems. Canadian
Mathematical Bulletin. Canadian Mathematical Society. https://doi.org/10.4153/s000843952000096x
chicago: Ivanov, Grigory. “Tight Frames and Related Geometric Problems.” Canadian
Mathematical Bulletin. Canadian Mathematical Society, 2021. https://doi.org/10.4153/s000843952000096x.
ieee: G. Ivanov, “Tight frames and related geometric problems,” Canadian Mathematical
Bulletin, vol. 64, no. 4. Canadian Mathematical Society, pp. 942–963, 2021.
ista: Ivanov G. 2021. Tight frames and related geometric problems. Canadian Mathematical
Bulletin. 64(4), 942–963.
mla: Ivanov, Grigory. “Tight Frames and Related Geometric Problems.” Canadian
Mathematical Bulletin, vol. 64, no. 4, Canadian Mathematical Society, 2021,
pp. 942–63, doi:10.4153/s000843952000096x.
short: G. Ivanov, Canadian Mathematical Bulletin 64 (2021) 942–963.
date_created: 2022-03-18T09:55:59Z
date_published: 2021-12-18T00:00:00Z
date_updated: 2023-09-05T12:43:09Z
day: '18'
department:
- _id: UlWa
doi: 10.4153/s000843952000096x
external_id:
arxiv:
- '1804.10055'
isi:
- '000730165300021'
intvolume: ' 64'
isi: 1
issue: '4'
keyword:
- General Mathematics
- Tight frame
- Grassmannian
- zonotope
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1804.10055
month: '12'
oa: 1
oa_version: Preprint
page: 942-963
publication: Canadian Mathematical Bulletin
publication_identifier:
eissn:
- 1496-4287
issn:
- 0008-4395
publication_status: published
publisher: Canadian Mathematical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Tight frames and related geometric problems
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 64
year: '2021'
...
---
_id: '9290'
abstract:
- lang: eng
text: Polar subcellular localization of the PIN exporters of the phytohormone auxin
is a key determinant of directional, intercellular auxin transport and thus a
central topic of both plant cell and developmental biology. Arabidopsis mutants
lacking PID, a kinase that phosphorylates PINs, or the MAB4/MEL proteins of unknown
molecular function display PIN polarity defects and phenocopy pin mutants, but
mechanistic insights into how these factors convey PIN polarity are missing. Here,
by combining protein biochemistry with quantitative live-cell imaging, we demonstrate
that PINs, MAB4/MELs, and AGC kinases interact in the same complex at the plasma
membrane. MAB4/MELs are recruited to the plasma membrane by the PINs and in concert
with the AGC kinases maintain PIN polarity through limiting lateral diffusion-based
escape of PINs from the polar domain. The PIN-MAB4/MEL-PID protein complex has
self-reinforcing properties thanks to positive feedback between AGC kinase-mediated
PIN phosphorylation and MAB4/MEL recruitment. We thus uncover the molecular mechanism
by which AGC kinases and MAB4/MEL proteins regulate PIN localization and plant
development.
acknowledged_ssus:
- _id: Bio
acknowledgement: We acknowledge Ben Scheres, Christian Luschnig, and Claus Schwechheimer
for sharing published material. We thank Monika Hrtyan and Dorota Jaworska at IST
Austria and Gerda Lamers and Ward de Winter at IBL Netherlands for technical assistance;
Corinna Hartinger, Jakub Hajný, Lesia Rodriguez, Mingyue Li, and Lindy Abas for
experimental support; and the Bioimaging Facility at IST Austria and the Bioimaging
Core at VIB for imaging support. We are grateful to Christian Luschnig, Lindy Abas,
and Roman Pleskot for valuable discussions. We also acknowledge the EMBO for supporting
M.G. with a long-term fellowship ( ALTF 1005-2019 ) during the finalization and
revision of this manuscript in the laboratory of B.D.R., and we thank R. Pierik
for allowing K.V.G. to work on this manuscript during a postdoc in his laboratory
at Utrecht University. This work was supported by grants from the European Research
Council under the European Union’s Seventh Framework Programme (ERC grant agreements
742985 to J.F., 714055 to B.D.R., and 803048 to M.F.), the Austrian Science Fund
(FWF; I 3630-B25 to J.F.), Chemical Sciences (partly) financed by the Dutch Research
Council (NWO-CW TOP 700.58.301 to R.O.), the Dutch Research Council (NWO-VICI 865.17.002
to R. Pierik), Grants-in-Aid from the Ministry of Education, Culture, Sports, Science
and Technology, Japan (KAKENHI grant 17K17595 to S.N.), the Ministry of Education,
Youth and Sports of the Czech Republic (MŠMT project NPUI-LO1417 ), and a China
Scholarship Council (to X.W.).
article_processing_charge: No
article_type: original
author:
- first_name: Matous
full_name: Glanc, Matous
id: 1AE1EA24-02D0-11E9-9BAA-DAF4881429F2
last_name: Glanc
orcid: 0000-0003-0619-7783
- first_name: K
full_name: Van Gelderen, K
last_name: Van Gelderen
- first_name: Lukas
full_name: Hörmayer, Lukas
id: 2EEE7A2A-F248-11E8-B48F-1D18A9856A87
last_name: Hörmayer
orcid: 0000-0001-8295-2926
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: S
full_name: Naramoto, S
last_name: Naramoto
- first_name: Xixi
full_name: Zhang, Xixi
id: 61A66458-47E9-11EA-85BA-8AEAAF14E49A
last_name: Zhang
orcid: 0000-0001-7048-4627
- first_name: David
full_name: Domjan, David
id: C684CD7A-257E-11EA-9B6F-D8588B4F947F
last_name: Domjan
orcid: 0000-0003-2267-106X
- first_name: L
full_name: Vcelarova, L
last_name: Vcelarova
- first_name: Robert
full_name: Hauschild, Robert
id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
last_name: Hauschild
orcid: 0000-0001-9843-3522
- first_name: Alexander J
full_name: Johnson, Alexander J
id: 46A62C3A-F248-11E8-B48F-1D18A9856A87
last_name: Johnson
orcid: 0000-0002-2739-8843
- first_name: E
full_name: de Koning, E
last_name: de Koning
- first_name: M
full_name: van Dop, M
last_name: van Dop
- first_name: E
full_name: Rademacher, E
last_name: Rademacher
- first_name: S
full_name: Janson, S
last_name: Janson
- first_name: X
full_name: Wei, X
last_name: Wei
- first_name: Gergely
full_name: Molnar, Gergely
id: 34F1AF46-F248-11E8-B48F-1D18A9856A87
last_name: Molnar
- first_name: Matyas
full_name: Fendrych, Matyas
id: 43905548-F248-11E8-B48F-1D18A9856A87
last_name: Fendrych
orcid: 0000-0002-9767-8699
- first_name: B
full_name: De Rybel, B
last_name: De Rybel
- first_name: R
full_name: Offringa, R
last_name: Offringa
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Glanc M, Van Gelderen K, Hörmayer L, et al. AGC kinases and MAB4/MEL proteins
maintain PIN polarity by limiting lateral diffusion in plant cells. Current
Biology. 2021;31(9):1918-1930. doi:10.1016/j.cub.2021.02.028
apa: Glanc, M., Van Gelderen, K., Hörmayer, L., Tan, S., Naramoto, S., Zhang, X.,
… Friml, J. (2021). AGC kinases and MAB4/MEL proteins maintain PIN polarity by
limiting lateral diffusion in plant cells. Current Biology. Elsevier. https://doi.org/10.1016/j.cub.2021.02.028
chicago: Glanc, Matous, K Van Gelderen, Lukas Hörmayer, Shutang Tan, S Naramoto,
Xixi Zhang, David Domjan, et al. “AGC Kinases and MAB4/MEL Proteins Maintain PIN
Polarity by Limiting Lateral Diffusion in Plant Cells.” Current Biology.
Elsevier, 2021. https://doi.org/10.1016/j.cub.2021.02.028.
ieee: M. Glanc et al., “AGC kinases and MAB4/MEL proteins maintain PIN polarity
by limiting lateral diffusion in plant cells,” Current Biology, vol. 31,
no. 9. Elsevier, pp. 1918–1930, 2021.
ista: Glanc M, Van Gelderen K, Hörmayer L, Tan S, Naramoto S, Zhang X, Domjan D,
Vcelarova L, Hauschild R, Johnson AJ, de Koning E, van Dop M, Rademacher E, Janson
S, Wei X, Molnar G, Fendrych M, De Rybel B, Offringa R, Friml J. 2021. AGC kinases
and MAB4/MEL proteins maintain PIN polarity by limiting lateral diffusion in plant
cells. Current Biology. 31(9), 1918–1930.
mla: Glanc, Matous, et al. “AGC Kinases and MAB4/MEL Proteins Maintain PIN Polarity
by Limiting Lateral Diffusion in Plant Cells.” Current Biology, vol. 31,
no. 9, Elsevier, 2021, pp. 1918–30, doi:10.1016/j.cub.2021.02.028.
short: M. Glanc, K. Van Gelderen, L. Hörmayer, S. Tan, S. Naramoto, X. Zhang, D.
Domjan, L. Vcelarova, R. Hauschild, A.J. Johnson, E. de Koning, M. van Dop, E.
Rademacher, S. Janson, X. Wei, G. Molnar, M. Fendrych, B. De Rybel, R. Offringa,
J. Friml, Current Biology 31 (2021) 1918–1930.
date_created: 2021-03-26T12:09:33Z
date_published: 2021-03-10T00:00:00Z
date_updated: 2023-09-05T13:03:34Z
day: '10'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.cub.2021.02.028
ec_funded: 1
external_id:
isi:
- '000653077800004'
pmid:
- '33705718'
file:
- access_level: open_access
checksum: b1723040ecfd8c81194185472eb62546
content_type: application/pdf
creator: dernst
date_created: 2021-04-01T10:53:42Z
date_updated: 2021-04-01T10:53:42Z
file_id: '9303'
file_name: 2021_CurrentBiology_Glanc.pdf
file_size: 4324371
relation: main_file
success: 1
file_date_updated: 2021-04-01T10:53:42Z
has_accepted_license: '1'
intvolume: ' 31'
isi: 1
issue: '9'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
page: 1918-1930
pmid: 1
project:
- _id: 261099A6-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '742985'
name: Tracing Evolution of Auxin Transport and Polarity in Plants
- _id: 26538374-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I03630
name: Molecular mechanisms of endocytic cargo recognition in plants
publication: Current Biology
publication_identifier:
eissn:
- 1879-0445
issn:
- 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: AGC kinases and MAB4/MEL proteins maintain PIN polarity by limiting lateral
diffusion in plant 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: 31
year: '2021'
...
---
_id: '8824'
abstract:
- lang: eng
text: Plants are able to orient their growth according to gravity, which ultimately
controls both shoot and root architecture.1 Gravitropism is a dynamic process
whereby gravistimulation induces the asymmetric distribution of the plant hormone
auxin, leading to asymmetric growth, organ bending, and subsequent reset of auxin
distribution back to the original pre-gravistimulation situation.1, 2, 3 Differential
auxin accumulation during the gravitropic response depends on the activity of
polarly localized PIN-FORMED (PIN) auxin-efflux carriers.1, 2, 3, 4 In particular,
the timing of this dynamic response is regulated by PIN2,5,6 but the underlying
molecular mechanisms are poorly understood. Here, we show that MEMBRANE ASSOCIATED
KINASE REGULATOR2 (MAKR2) controls the pace of the root gravitropic response.
We found that MAKR2 is required for the PIN2 asymmetry during gravitropism by
acting as a negative regulator of the cell-surface signaling mediated by the receptor-like
kinase TRANSMEMBRANE KINASE1 (TMK1).2,7, 8, 9, 10 Furthermore, we show that
the MAKR2 inhibitory effect on TMK1 signaling is antagonized by auxin itself,
which triggers rapid MAKR2 membrane dissociation in a TMK1-dependent manner. Our
findings suggest that the timing of the root gravitropic response is orchestrated
by the reversible inhibition of the TMK1 signaling pathway at the cell surface.
acknowledgement: "We thank the SiCE group for discussions and comments; S. Yalovsky,
B. Scheres, and the NASC/ABRC collection for providing transgenic Arabidopsis lines
and plasmids; L. Kalmbach and M. Barberon for the gift of pLOK180_pFR7m34GW; A.
Lacroix, J. Berger, and P. Bolland for plant care; and M. Fendrych for help with
microfluidics in the J.F. lab. We acknowledge\r\nthe contribution of the SFR Biosciences
(UMS3444/CNRS, US8/Inser m, ENS de Lyon, UCBL) facilities: C. Lionet, E. Chatre,
and J. Brocard at LBIPLATIM-MICROSCOPY for assistance with imaging, and V. GuegenChaignon
and A. Page at the Protein Science Facility (PSF) for assistance with protein purification
and mass spectrometry. Y.J. was funded by ERC\r\ngrant 3363360-APPL under FP/2007–2013.
Y.J. and Z.L.N. were funded by an ANR- and NSF-supported ERA-CAPS project (SICOPID:
ANR-17-CAPS0003-01/NSF PGRP IOS-1841917). A.I.C.-D. is funded by an ERC consolidator
grant (ERC-2015-CoG–683163) and BIO2016-78955 grant from the Spanish Ministry of
Economy and Competitiveness. Exchanges between the Y.J. and T.B. laboratories were
funded by Tournesol grant 35656NB. B.K.M. was\r\nfunded by the Omics@vib Marie Curie
COFUND and Research Foundation Flanders for a postdoctoral fellowship."
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: MM
full_name: Marquès-Bueno, MM
last_name: Marquès-Bueno
- first_name: L
full_name: Armengot, L
last_name: Armengot
- first_name: LC
full_name: Noack, LC
last_name: Noack
- first_name: J
full_name: Bareille, J
last_name: Bareille
- first_name: Lesia
full_name: Rodriguez Solovey, Lesia
id: 3922B506-F248-11E8-B48F-1D18A9856A87
last_name: Rodriguez Solovey
orcid: 0000-0002-7244-7237
- first_name: MP
full_name: Platre, MP
last_name: Platre
- first_name: V
full_name: Bayle, V
last_name: Bayle
- first_name: M
full_name: Liu, M
last_name: Liu
- first_name: D
full_name: Opdenacker, D
last_name: Opdenacker
- first_name: S
full_name: Vanneste, S
last_name: Vanneste
- first_name: BK
full_name: Möller, BK
last_name: Möller
- first_name: ZL
full_name: Nimchuk, ZL
last_name: Nimchuk
- first_name: T
full_name: Beeckman, T
last_name: Beeckman
- first_name: AI
full_name: Caño-Delgado, AI
last_name: Caño-Delgado
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Y
full_name: Jaillais, Y
last_name: Jaillais
citation:
ama: Marquès-Bueno M, Armengot L, Noack L, et al. Auxin-regulated reversible inhibition
of TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism. Current
Biology. 2021;31(1). doi:10.1016/j.cub.2020.10.011
apa: Marquès-Bueno, M., Armengot, L., Noack, L., Bareille, J., Rodriguez Solovey,
L., Platre, M., … Jaillais, Y. (2021). Auxin-regulated reversible inhibition of
TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism. Current
Biology. Elsevier. https://doi.org/10.1016/j.cub.2020.10.011
chicago: Marquès-Bueno, MM, L Armengot, LC Noack, J Bareille, Lesia Rodriguez Solovey,
MP Platre, V Bayle, et al. “Auxin-Regulated Reversible Inhibition of TMK1 Signaling
by MAKR2 Modulates the Dynamics of Root Gravitropism.” Current Biology.
Elsevier, 2021. https://doi.org/10.1016/j.cub.2020.10.011.
ieee: M. Marquès-Bueno et al., “Auxin-regulated reversible inhibition of
TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism,” Current
Biology, vol. 31, no. 1. Elsevier, 2021.
ista: Marquès-Bueno M, Armengot L, Noack L, Bareille J, Rodriguez Solovey L, Platre
M, Bayle V, Liu M, Opdenacker D, Vanneste S, Möller B, Nimchuk Z, Beeckman T,
Caño-Delgado A, Friml J, Jaillais Y. 2021. Auxin-regulated reversible inhibition
of TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism. Current
Biology. 31(1).
mla: Marquès-Bueno, MM, et al. “Auxin-Regulated Reversible Inhibition of TMK1 Signaling
by MAKR2 Modulates the Dynamics of Root Gravitropism.” Current Biology,
vol. 31, no. 1, Elsevier, 2021, doi:10.1016/j.cub.2020.10.011.
short: M. Marquès-Bueno, L. Armengot, L. Noack, J. Bareille, L. Rodriguez Solovey,
M. Platre, V. Bayle, M. Liu, D. Opdenacker, S. Vanneste, B. Möller, Z. Nimchuk,
T. Beeckman, A. Caño-Delgado, J. Friml, Y. Jaillais, Current Biology 31 (2021).
date_created: 2020-12-01T13:39:46Z
date_published: 2021-01-11T00:00:00Z
date_updated: 2023-09-05T13:03:15Z
day: '11'
ddc:
- '570'
department:
- _id: JiFr
doi: 10.1016/j.cub.2020.10.011
external_id:
isi:
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pmid:
- '33157019'
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publication_identifier:
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publisher: Elsevier
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title: Auxin-regulated reversible inhibition of TMK1 signaling by MAKR2 modulates
the dynamics of root gravitropism
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legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
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