---
_id: '8402'
abstract:
- lang: eng
text: "Background: The mitochondrial pyruvate carrier (MPC) plays a central role
in energy metabolism by transporting pyruvate across the inner mitochondrial membrane.
Its heterodimeric composition and homology to SWEET and semiSWEET transporters
set the MPC apart from the canonical mitochondrial carrier family (named MCF or
SLC25). The import of the canonical carriers is mediated by the carrier translocase
of the inner membrane (TIM22) pathway and is dependent on their structure, which
features an even number of transmembrane segments and both termini in the intermembrane
space. The import pathway of MPC proteins has not been elucidated. The odd number
of transmembrane segments and positioning of the N-terminus in the matrix argues
against an import via the TIM22 carrier pathway but favors an import via the flexible
presequence pathway.\r\nResults: Here, we systematically analyzed the import pathways
of Mpc2 and Mpc3 and report that, contrary to an expected import via the flexible
presequence pathway, yeast MPC proteins with an odd number of transmembrane segments
and matrix-exposed N-terminus are imported by the carrier pathway, using the receptor
Tom70, small TIM chaperones, and the TIM22 complex. The TIM9·10 complex chaperones
MPC proteins through the mitochondrial intermembrane space using conserved hydrophobic
motifs that are also required for the interaction with canonical carrier proteins.\r\nConclusions:
The carrier pathway can import paired and non-paired transmembrane helices and
translocate N-termini to either side of the mitochondrial inner membrane, revealing
an unexpected versatility of the mitochondrial import pathway for non-cleavable
inner membrane proteins."
article_number: '2'
article_processing_charge: No
article_type: original
author:
- first_name: Heike
full_name: Rampelt, Heike
last_name: Rampelt
- first_name: Iva
full_name: Sucec, Iva
last_name: Sucec
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Patrick
full_name: Horten, Patrick
last_name: Horten
- first_name: Inge
full_name: Perschil, Inge
last_name: Perschil
- first_name: Jean-Claude
full_name: Martinou, Jean-Claude
last_name: Martinou
- first_name: Martin
full_name: van der Laan, Martin
last_name: van der Laan
- first_name: Nils
full_name: Wiedemann, Nils
last_name: Wiedemann
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Nikolaus
full_name: Pfanner, Nikolaus
last_name: Pfanner
citation:
ama: Rampelt H, Sucec I, Bersch B, et al. The mitochondrial carrier pathway transports
non-canonical substrates with an odd number of transmembrane segments. BMC
Biology. 2020;18. doi:10.1186/s12915-019-0733-6
apa: Rampelt, H., Sucec, I., Bersch, B., Horten, P., Perschil, I., Martinou, J.-C.,
… Pfanner, N. (2020). The mitochondrial carrier pathway transports non-canonical
substrates with an odd number of transmembrane segments. BMC Biology. Springer
Nature. https://doi.org/10.1186/s12915-019-0733-6
chicago: Rampelt, Heike, Iva Sucec, Beate Bersch, Patrick Horten, Inge Perschil,
Jean-Claude Martinou, Martin van der Laan, Nils Wiedemann, Paul Schanda, and Nikolaus
Pfanner. “The Mitochondrial Carrier Pathway Transports Non-Canonical Substrates
with an Odd Number of Transmembrane Segments.” BMC Biology. Springer Nature,
2020. https://doi.org/10.1186/s12915-019-0733-6.
ieee: H. Rampelt et al., “The mitochondrial carrier pathway transports non-canonical
substrates with an odd number of transmembrane segments,” BMC Biology,
vol. 18. Springer Nature, 2020.
ista: Rampelt H, Sucec I, Bersch B, Horten P, Perschil I, Martinou J-C, van der
Laan M, Wiedemann N, Schanda P, Pfanner N. 2020. The mitochondrial carrier pathway
transports non-canonical substrates with an odd number of transmembrane segments.
BMC Biology. 18, 2.
mla: Rampelt, Heike, et al. “The Mitochondrial Carrier Pathway Transports Non-Canonical
Substrates with an Odd Number of Transmembrane Segments.” BMC Biology,
vol. 18, 2, Springer Nature, 2020, doi:10.1186/s12915-019-0733-6.
short: H. Rampelt, I. Sucec, B. Bersch, P. Horten, I. Perschil, J.-C. Martinou,
M. van der Laan, N. Wiedemann, P. Schanda, N. Pfanner, BMC Biology 18 (2020).
date_created: 2020-09-17T10:26:53Z
date_published: 2020-01-06T00:00:00Z
date_updated: 2021-01-12T08:19:02Z
day: '06'
doi: 10.1186/s12915-019-0733-6
extern: '1'
external_id:
pmid:
- '31907035'
intvolume: ' 18'
keyword:
- Biotechnology
- Plant Science
- General Biochemistry
- Genetics and Molecular Biology
- Developmental Biology
- Cell Biology
- Physiology
- Ecology
- Evolution
- Behavior and Systematics
- Structural Biology
- General Agricultural and Biological Sciences
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1186/s12915-019-0733-6
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
publication: BMC Biology
publication_identifier:
issn:
- 1741-7007
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: The mitochondrial carrier pathway transports non-canonical substrates with
an odd number of transmembrane segments
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 18
year: '2020'
...
---
_id: '10354'
abstract:
- lang: eng
text: "Background\r\nESCRT-III is a membrane remodelling filament with the unique
ability to cut membranes from the inside of the membrane neck. It is essential
for the final stage of cell division, the formation of vesicles, the release of
viruses, and membrane repair. Distinct from other cytoskeletal filaments, ESCRT-III
filaments do not consume energy themselves, but work in conjunction with another
ATP-consuming complex. Despite rapid progress in describing the cell biology of
ESCRT-III, we lack an understanding of the physical mechanisms behind its force
production and membrane remodelling.\r\nResults\r\nHere we present a minimal coarse-grained
model that captures all the experimentally reported cases of ESCRT-III driven
membrane sculpting, including the formation of downward and upward cones and tubules.
This model suggests that a change in the geometry of membrane bound ESCRT-III
filaments—from a flat spiral to a 3D helix—drives membrane deformation. We then
show that such repetitive filament geometry transitions can induce the fission
of cargo-containing vesicles.\r\nConclusions\r\nOur model provides a general physical
mechanism that explains the full range of ESCRT-III-dependent membrane remodelling
and scission events observed in cells. This mechanism for filament force production
is distinct from the mechanisms described for other cytoskeletal elements discovered
so far. The mechanistic principles revealed here suggest new ways of manipulating
ESCRT-III-driven processes in cells and could be used to guide the engineering
of synthetic membrane-sculpting systems."
acknowledgement: We thank Jeremy Carlton, Mike Staddon, Geraint Harker, and the Wellcome
Trust Consortium “Archaeal Origins of Eukaryotic Cell Organisation” for fruitful
conversations. We thank Peter Wirnsberger and Tine Curk for discussions about the
membrane model implementation.
article_number: '82'
article_processing_charge: No
article_type: original
author:
- first_name: Lena
full_name: Harker-Kirschneck, Lena
last_name: Harker-Kirschneck
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Harker-Kirschneck L, Baum B, Šarić A. Changes in ESCRT-III filament geometry
drive membrane remodelling and fission in silico. BMC Biology. 2019;17(1).
doi:10.1186/s12915-019-0700-2
apa: Harker-Kirschneck, L., Baum, B., & Šarić, A. (2019). Changes in ESCRT-III
filament geometry drive membrane remodelling and fission in silico. BMC Biology.
Springer Nature. https://doi.org/10.1186/s12915-019-0700-2
chicago: Harker-Kirschneck, Lena, Buzz Baum, and Anđela Šarić. “Changes in ESCRT-III
Filament Geometry Drive Membrane Remodelling and Fission in Silico.” BMC Biology.
Springer Nature, 2019. https://doi.org/10.1186/s12915-019-0700-2.
ieee: L. Harker-Kirschneck, B. Baum, and A. Šarić, “Changes in ESCRT-III filament
geometry drive membrane remodelling and fission in silico,” BMC Biology,
vol. 17, no. 1. Springer Nature, 2019.
ista: Harker-Kirschneck L, Baum B, Šarić A. 2019. Changes in ESCRT-III filament
geometry drive membrane remodelling and fission in silico. BMC Biology. 17(1),
82.
mla: Harker-Kirschneck, Lena, et al. “Changes in ESCRT-III Filament Geometry Drive
Membrane Remodelling and Fission in Silico.” BMC Biology, vol. 17, no.
1, 82, Springer Nature, 2019, doi:10.1186/s12915-019-0700-2.
short: L. Harker-Kirschneck, B. Baum, A. Šarić, BMC Biology 17 (2019).
date_created: 2021-11-26T11:25:03Z
date_published: 2019-10-22T00:00:00Z
date_updated: 2021-11-26T11:54:29Z
day: '22'
ddc:
- '570'
doi: 10.1186/s12915-019-0700-2
extern: '1'
external_id:
pmid:
- '31640700'
file:
- access_level: open_access
checksum: 31d8bae55a376d30925f53f7e1a02396
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-26T11:37:54Z
date_updated: 2021-11-26T11:37:54Z
file_id: '10356'
file_name: 2019_BMCBio_Harker_Kirschneck.pdf
file_size: 1648926
relation: main_file
success: 1
file_date_updated: 2021-11-26T11:37:54Z
has_accepted_license: '1'
intvolume: ' 17'
issue: '1'
keyword:
- cell biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/559898
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
publication: BMC Biology
publication_identifier:
issn:
- 1741-7007
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Changes in ESCRT-III filament geometry drive membrane remodelling and fission
in silico
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: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 17
year: '2019'
...