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Cooperation of translocase complexes in mitochondrial protein import
Most mitochondrial proteins are synthesized in the cytosol and imported into one of the four mitochondrial compartments: outer membrane, intermembrane space, inner membrane, and matrix. Each compartment contains protein complexes that interact with precursor proteins and promote their transport. The...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2080918/ https://www.ncbi.nlm.nih.gov/pubmed/17998403 http://dx.doi.org/10.1083/jcb.200708199 |
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author | Kutik, Stephan Guiard, Bernard Meyer, Helmut E. Wiedemann, Nils Pfanner, Nikolaus |
author_facet | Kutik, Stephan Guiard, Bernard Meyer, Helmut E. Wiedemann, Nils Pfanner, Nikolaus |
author_sort | Kutik, Stephan |
collection | PubMed |
description | Most mitochondrial proteins are synthesized in the cytosol and imported into one of the four mitochondrial compartments: outer membrane, intermembrane space, inner membrane, and matrix. Each compartment contains protein complexes that interact with precursor proteins and promote their transport. These translocase complexes do not act as independent units but cooperate with each other and further membrane complexes in a dynamic manner. We propose that a regulated coupling of translocases is important for the coordination of preprotein translocation and efficient sorting to intramitochondrial compartments. |
format | Text |
id | pubmed-2080918 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-20809182008-05-19 Cooperation of translocase complexes in mitochondrial protein import Kutik, Stephan Guiard, Bernard Meyer, Helmut E. Wiedemann, Nils Pfanner, Nikolaus J Cell Biol Reviews Most mitochondrial proteins are synthesized in the cytosol and imported into one of the four mitochondrial compartments: outer membrane, intermembrane space, inner membrane, and matrix. Each compartment contains protein complexes that interact with precursor proteins and promote their transport. These translocase complexes do not act as independent units but cooperate with each other and further membrane complexes in a dynamic manner. We propose that a regulated coupling of translocases is important for the coordination of preprotein translocation and efficient sorting to intramitochondrial compartments. The Rockefeller University Press 2007-11-19 /pmc/articles/PMC2080918/ /pubmed/17998403 http://dx.doi.org/10.1083/jcb.200708199 Text en Copyright © 2007, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Reviews Kutik, Stephan Guiard, Bernard Meyer, Helmut E. Wiedemann, Nils Pfanner, Nikolaus Cooperation of translocase complexes in mitochondrial protein import |
title | Cooperation of translocase complexes in mitochondrial protein import |
title_full | Cooperation of translocase complexes in mitochondrial protein import |
title_fullStr | Cooperation of translocase complexes in mitochondrial protein import |
title_full_unstemmed | Cooperation of translocase complexes in mitochondrial protein import |
title_short | Cooperation of translocase complexes in mitochondrial protein import |
title_sort | cooperation of translocase complexes in mitochondrial protein import |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2080918/ https://www.ncbi.nlm.nih.gov/pubmed/17998403 http://dx.doi.org/10.1083/jcb.200708199 |
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