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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...

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Detalles Bibliográficos
Autores principales: Kutik, Stephan, Guiard, Bernard, Meyer, Helmut E., Wiedemann, Nils, Pfanner, Nikolaus
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2007
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.
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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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