---
_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. <i>BMC
    Biology</i>. 2020;18. doi:<a href="https://doi.org/10.1186/s12915-019-0733-6">10.1186/s12915-019-0733-6</a>
  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. <i>BMC Biology</i>. Springer
    Nature. <a href="https://doi.org/10.1186/s12915-019-0733-6">https://doi.org/10.1186/s12915-019-0733-6</a>
  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.” <i>BMC Biology</i>. Springer Nature,
    2020. <a href="https://doi.org/10.1186/s12915-019-0733-6">https://doi.org/10.1186/s12915-019-0733-6</a>.
  ieee: H. Rampelt <i>et al.</i>, “The mitochondrial carrier pathway transports non-canonical
    substrates with an odd number of transmembrane segments,” <i>BMC Biology</i>,
    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.” <i>BMC Biology</i>,
    vol. 18, 2, Springer Nature, 2020, doi:<a href="https://doi.org/10.1186/s12915-019-0733-6">10.1186/s12915-019-0733-6</a>.
  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. <i>BMC Biology</i>. 2019;17(1).
    doi:<a href="https://doi.org/10.1186/s12915-019-0700-2">10.1186/s12915-019-0700-2</a>
  apa: Harker-Kirschneck, L., Baum, B., &#38; Šarić, A. (2019). Changes in ESCRT-III
    filament geometry drive membrane remodelling and fission in silico. <i>BMC Biology</i>.
    Springer Nature. <a href="https://doi.org/10.1186/s12915-019-0700-2">https://doi.org/10.1186/s12915-019-0700-2</a>
  chicago: Harker-Kirschneck, Lena, Buzz Baum, and Anđela Šarić. “Changes in ESCRT-III
    Filament Geometry Drive Membrane Remodelling and Fission in Silico.” <i>BMC Biology</i>.
    Springer Nature, 2019. <a href="https://doi.org/10.1186/s12915-019-0700-2">https://doi.org/10.1186/s12915-019-0700-2</a>.
  ieee: L. Harker-Kirschneck, B. Baum, and A. Šarić, “Changes in ESCRT-III filament
    geometry drive membrane remodelling and fission in silico,” <i>BMC Biology</i>,
    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.” <i>BMC Biology</i>, vol. 17, no.
    1, 82, Springer Nature, 2019, doi:<a href="https://doi.org/10.1186/s12915-019-0700-2">10.1186/s12915-019-0700-2</a>.
  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
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'
...