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Identification of new channels by systematic analysis of the mitochondrial outer membrane

The mitochondrial outer membrane is essential for communication between mitochondria and the rest of the cell and facilitates the transport of metabolites, ions, and proteins. All mitochondrial outer membrane channels known to date are β-barrel membrane proteins, including the abundant voltage-depen...

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Autores principales: Krüger, Vivien, Becker, Thomas, Becker, Lars, Montilla-Martinez, Malayko, Ellenrieder, Lars, Vögtle, F.-Nora, Meyer, Helmut E., Ryan, Michael T., Wiedemann, Nils, Warscheid, Bettina, Pfanner, Nikolaus, Wagner, Richard, Meisinger, Chris
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5674900/
https://www.ncbi.nlm.nih.gov/pubmed/28916712
http://dx.doi.org/10.1083/jcb.201706043
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author Krüger, Vivien
Becker, Thomas
Becker, Lars
Montilla-Martinez, Malayko
Ellenrieder, Lars
Vögtle, F.-Nora
Meyer, Helmut E.
Ryan, Michael T.
Wiedemann, Nils
Warscheid, Bettina
Pfanner, Nikolaus
Wagner, Richard
Meisinger, Chris
author_facet Krüger, Vivien
Becker, Thomas
Becker, Lars
Montilla-Martinez, Malayko
Ellenrieder, Lars
Vögtle, F.-Nora
Meyer, Helmut E.
Ryan, Michael T.
Wiedemann, Nils
Warscheid, Bettina
Pfanner, Nikolaus
Wagner, Richard
Meisinger, Chris
author_sort Krüger, Vivien
collection PubMed
description The mitochondrial outer membrane is essential for communication between mitochondria and the rest of the cell and facilitates the transport of metabolites, ions, and proteins. All mitochondrial outer membrane channels known to date are β-barrel membrane proteins, including the abundant voltage-dependent anion channel and the cation-preferring protein-conducting channels Tom40, Sam50, and Mdm10. We analyzed outer membrane fractions of yeast mitochondria and identified four new channel activities: two anion-preferring channels and two cation-preferring channels. We characterized the cation-preferring channels at the molecular level. The mitochondrial import component Mim1 forms a channel that is predicted to have an α-helical structure for protein import. The short-chain dehydrogenase-related protein Ayr1 forms an NADPH-regulated channel. We conclude that the mitochondrial outer membrane contains a considerably larger variety of channel-forming proteins than assumed thus far. These findings challenge the traditional view of the outer membrane as an unspecific molecular sieve and indicate a higher degree of selectivity and regulation of metabolite fluxes at the mitochondrial boundary.
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spelling pubmed-56749002017-11-08 Identification of new channels by systematic analysis of the mitochondrial outer membrane Krüger, Vivien Becker, Thomas Becker, Lars Montilla-Martinez, Malayko Ellenrieder, Lars Vögtle, F.-Nora Meyer, Helmut E. Ryan, Michael T. Wiedemann, Nils Warscheid, Bettina Pfanner, Nikolaus Wagner, Richard Meisinger, Chris J Cell Biol Research Articles The mitochondrial outer membrane is essential for communication between mitochondria and the rest of the cell and facilitates the transport of metabolites, ions, and proteins. All mitochondrial outer membrane channels known to date are β-barrel membrane proteins, including the abundant voltage-dependent anion channel and the cation-preferring protein-conducting channels Tom40, Sam50, and Mdm10. We analyzed outer membrane fractions of yeast mitochondria and identified four new channel activities: two anion-preferring channels and two cation-preferring channels. We characterized the cation-preferring channels at the molecular level. The mitochondrial import component Mim1 forms a channel that is predicted to have an α-helical structure for protein import. The short-chain dehydrogenase-related protein Ayr1 forms an NADPH-regulated channel. We conclude that the mitochondrial outer membrane contains a considerably larger variety of channel-forming proteins than assumed thus far. These findings challenge the traditional view of the outer membrane as an unspecific molecular sieve and indicate a higher degree of selectivity and regulation of metabolite fluxes at the mitochondrial boundary. The Rockefeller University Press 2017-11-06 /pmc/articles/PMC5674900/ /pubmed/28916712 http://dx.doi.org/10.1083/jcb.201706043 Text en © 2017 Krüger et al. https://creativecommons.org/licenses/by/4.0/This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Articles
Krüger, Vivien
Becker, Thomas
Becker, Lars
Montilla-Martinez, Malayko
Ellenrieder, Lars
Vögtle, F.-Nora
Meyer, Helmut E.
Ryan, Michael T.
Wiedemann, Nils
Warscheid, Bettina
Pfanner, Nikolaus
Wagner, Richard
Meisinger, Chris
Identification of new channels by systematic analysis of the mitochondrial outer membrane
title Identification of new channels by systematic analysis of the mitochondrial outer membrane
title_full Identification of new channels by systematic analysis of the mitochondrial outer membrane
title_fullStr Identification of new channels by systematic analysis of the mitochondrial outer membrane
title_full_unstemmed Identification of new channels by systematic analysis of the mitochondrial outer membrane
title_short Identification of new channels by systematic analysis of the mitochondrial outer membrane
title_sort identification of new channels by systematic analysis of the mitochondrial outer membrane
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5674900/
https://www.ncbi.nlm.nih.gov/pubmed/28916712
http://dx.doi.org/10.1083/jcb.201706043
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