Identification of new channels by systematic analysis of the mitochondrial outer membrane
DC Element | Wert | Sprache |
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dc.contributor.author | Krueger, Vivien | |
dc.contributor.author | Becker, Thomas | |
dc.contributor.author | Becker, Lars | |
dc.contributor.author | Montilla-Martinez, Malayko | |
dc.contributor.author | Ellenrieder, Lars | |
dc.contributor.author | Voegtle, F. -Nora | |
dc.contributor.author | Meyer, Helmut E. | |
dc.contributor.author | Ryan, Michael T. | |
dc.contributor.author | Wiedemann, Nils | |
dc.contributor.author | Warscheid, Bettina | |
dc.contributor.author | Pfanner, Nikolaus | |
dc.contributor.author | Wagner, Richard | |
dc.contributor.author | Meisinger, Chris | |
dc.date.accessioned | 2021-12-23T16:22:05Z | - |
dc.date.available | 2021-12-23T16:22:05Z | - |
dc.date.issued | 2017 | |
dc.identifier.issn | 00219525 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/14154 | - |
dc.description.abstract | 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 beta-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 a-helical structure for protein import. The short-chain dehydrogenase-related protein Ayr1 forms an NAD PH-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. | |
dc.description.sponsorship | Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [BE 4679/2-1, ME 1921/2-1, ME 1921/4-1, PF 202/8-1, WA 681/2-1]; Sonderforschungsbereiche [746, 1140]; Research Training Group [2202]; Excellence Initiative of the German federal and state governments (GSC-4 Spemann Graduate School) [EXC 294 BIOSS]; European Research CouncilEuropean Research Council (ERC)European Commission [648235]; This work was supported by the Deutsche Forschungsgemeinschaft (BE 4679/2-1, ME 1921/2-1, ME 1921/4-1, PF 202/8-1, WA 681/2-1), the Sonderforschungsbereiche (746 and 1140), the Research Training Group (2202), the Excellence Initiative of the German federal and state governments (EXC 294 BIOSS, GSC-4 Spemann Graduate School), and the European Research Council Consolidator Grant (648235). Work included in this study has also been performed in partial fulfillment of the requirements for the doctoral theses of V. Kruger and L. Becker at the University of Osnabruck. | |
dc.language.iso | en | |
dc.publisher | ROCKEFELLER UNIV PRESS | |
dc.relation.ispartof | JOURNAL OF CELL BIOLOGY | |
dc.subject | BETA-BARREL PROTEINS | |
dc.subject | BIOGENESIS | |
dc.subject | Cell Biology | |
dc.subject | DEPENDENT ANION CHANNELS | |
dc.subject | EUKARYOTIC CELLS | |
dc.subject | IMPORT PORE | |
dc.subject | LIPID PARTICLES | |
dc.subject | PREPROTEIN TRANSLOCATION CHANNEL | |
dc.subject | SACCHAROMYCES-CEREVISIAE | |
dc.subject | TOM COMPLEX | |
dc.subject | YEAST | |
dc.title | Identification of new channels by systematic analysis of the mitochondrial outer membrane | |
dc.type | journal article | |
dc.identifier.doi | 10.1083/jcb.201706043 | |
dc.identifier.isi | ISI:000414609700010 | |
dc.description.volume | 216 | |
dc.description.issue | 11 | |
dc.description.startpage | 3485 | |
dc.description.endpage | 3495 | |
dc.contributor.orcid | 0000-0002-8326-3548 | |
dc.contributor.orcid | 0000-0003-2586-8829 | |
dc.contributor.orcid | 0000-0002-5062-3287 | |
dc.contributor.orcid | 0000-0001-5096-1975 | |
dc.contributor.orcid | 0000-0001-8305-6728 | |
dc.contributor.researcherid | AAV-7878-2021 | |
dc.contributor.researcherid | J-1110-2014 | |
dc.contributor.researcherid | AAS-9404-2020 | |
dc.contributor.researcherid | X-2152-2019 | |
dc.contributor.researcherid | T-4290-2017 | |
dc.identifier.eissn | 15408140 | |
dc.publisher.place | 950 THIRD AVE, 2ND FLR, NEW YORK, NY 10022 USA | |
dcterms.isPartOf.abbreviation | J. Cell Biol. | |
dcterms.oaStatus | Green Published, hybrid | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | WaRi703 | - |
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geprüft am 08.06.2024