%0 Journal Article %1 krugerIdentificationNewChannels2017 %A Krüger, Vivien %A Becker, Thomas %A Becker, Lars %A Montilla-Martinez, Malayko %A Ellenrieder, Lars %A Vögtle, F.-Nora %A Meyer, Helmut E. %A Ryan, Michael T. %A Wiedemann, Nils %A Warscheid, Bettina %A Pfanner, Nikolaus %A Wagner, Richard %A Meisinger, Chris %C United States %D 2017 %J The Journal of cell biology %K Biological Conformation Ester Hydrolases/chemistry/genetics/*metabolism,Membrane Membranes/*metabolism,NADP/metabolism,Protein Proteins/chemistry/genetics/*metabolism,Mitochondria/*enzymology,Mitochondrial Proteins/chemistry/genetics/*metabolism,Saccharomyces Transport,Carboxylic alpha-Helical,Saccharomyces cerevisiae cerevisiae/*enzymology/genetics,to_read %N 11 %P 3485--3495 %R 10.1083/jcb.201706043 %T Identification of New Channels by Systematic Analysis of the Mitochondrial Outer Membrane. %V 216 %X 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 $\alpha$-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.

@article{krugerIdentificationNewChannels2017, 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 {$\alpha$}-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.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {United States}, author = {Kr{\"u}ger, Vivien and Becker, Thomas and Becker, Lars and {Montilla-Martinez}, Malayko and Ellenrieder, Lars and V{\"o}gtle, F.-Nora and Meyer, Helmut E. and Ryan, Michael T. and Wiedemann, Nils and Warscheid, Bettina and Pfanner, Nikolaus and Wagner, Richard and Meisinger, Chris}, biburl = {https://www.bibsonomy.org/bibtex/2880da91c794f9fcedc26ad20a2275f73/warscheidlab}, copyright = {{\copyright} 2017 Kr{\"u}ger et al.}, doi = {10.1083/jcb.201706043}, interhash = {803a15b59aa7cc25dc0a70e1c0df088e}, intrahash = {880da91c794f9fcedc26ad20a2275f73}, issn = {1540-8140 0021-9525}, journal = {The Journal of cell biology}, keywords = {Biological Conformation Ester Hydrolases/chemistry/genetics/*metabolism,Membrane Membranes/*metabolism,NADP/metabolism,Protein Proteins/chemistry/genetics/*metabolism,Mitochondria/*enzymology,Mitochondrial Proteins/chemistry/genetics/*metabolism,Saccharomyces Transport,Carboxylic alpha-Helical,Saccharomyces cerevisiae cerevisiae/*enzymology/genetics,to_read}, langid = {english}, month = nov, number = 11, pages = {3485--3495}, pmcid = {PMC5674900}, pmid = {28916712}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Identification of New Channels by Systematic Analysis of the Mitochondrial Outer Membrane.}, volume = 216, year = 2017 }