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; Wiedemann, Nils; Warscheid, Bettina; Pfanner, Nikolaus; Wagner, Richard; Meisinger, Chris

doi:10.1083/jcb.201706043

Cited by 43 publications

(55 citation statements)

References 89 publications

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“…Fourth, three new channels have been discovered in outer membrane vesicles of yeast mitochondria. Two clearly distinguishable anion‐selective channel activities, OMC7 and OMC8, with pore diameters of roughly 15 Å were detected in mitochondrial outer membrane vesicles . The corresponding channel‐forming proteins remain to be identified.…”

Section: Channel‐forming Proteins In Metabolite Transportmentioning

confidence: 97%

“…Little is known on how the MIM machinery mediates protein biogenesis. Recent insights derived from the observation that Mim1 forms a highly cation‐selective channel with a maximal conductance of 580 pS that corresponds to a pore diameter of about 16 Å . Co‐reconstitution with Mim2 modulates the Mim1 channel activity but its cation‐selectivity persists .…”

Section: Channel‐forming Proteins In Protein Transportmentioning

confidence: 99%

“…Recent insights derived from the observation that Mim1 forms a highly cation‐selective channel with a maximal conductance of 580 pS that corresponds to a pore diameter of about 16 Å . Co‐reconstitution with Mim2 modulates the Mim1 channel activity but its cation‐selectivity persists . Mim1 and Mim2 are each embedded into the outer membrane via a single predicted α‐helical transmembrane segment .…”

Section: Channel‐forming Proteins In Protein Transportmentioning

confidence: 99%

“…The mitochondrial division and morphology protein 10 (Mdm10) forms a β‐barrel channel that mediates the biogenesis of the TOM complex . Mim1 of the mitochondrial import machinery (MIM) promotes biogenesis of α‐helical outer membrane proteins and constitutes the first outer membrane channel with a predicted α‐helical structure . In addition, the acyl‐dihydroxyacetone phosphate reductase (Ayr1) forms a NADPH‐regulated channel and two additional anion‐selective channels (OMC7 and OMC8) have been identified in mitochondrial outer membrane vesicles .…”

Section: Introductionmentioning

confidence: 99%

“…Mim1 of the mitochondrial import machinery (MIM) promotes biogenesis of α‐helical outer membrane proteins and constitutes the first outer membrane channel with a predicted α‐helical structure . In addition, the acyl‐dihydroxyacetone phosphate reductase (Ayr1) forms a NADPH‐regulated channel and two additional anion‐selective channels (OMC7 and OMC8) have been identified in mitochondrial outer membrane vesicles . The transported substrates of these channels however are yet not known.…”

Section: Introductionmentioning

confidence: 99%

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Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

Becker

Wagner

2018

BioEssays

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Mitochondrial function and biogenesis depend on the transport of a large variety of proteins, ions, and metabolites across the two surrounding membranes. While several specific transporters are present in the inner membrane, transport processes across the outer membrane are less understood. Recent studies reveal that the number of outer membrane channels and their transport mechanisms are more diverse than originally thought. Four protein-conducting channels promote transport of distinct sets of precursor proteins across and into the outer membrane. The voltage-dependent anion channel (VDAC) forms the major channel for small hydrophilic molecules. In addition, three channels with yet unknown substrate specificity exist in the outer membrane. In this review, we outline the emerging functional diversity, selectivity, and regulation of mitochondrial outer membrane channels. The presence of several channel-forming proteins challenges the traditional view that the outer membrane forms an unspecific size-exclusion filter for the flux of small hydrophilic molecules.

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Section: Channel‐forming Proteins In Metabolite Transportmentioning

confidence: 97%

Section: Channel‐forming Proteins In Protein Transportmentioning

confidence: 99%

Section: Channel‐forming Proteins In Protein Transportmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

Becker

Wagner

2018

BioEssays

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Protein insertion into the inner membrane of mitochondria: routes and mechanisms

Kizmaz,

Nutz,

Egeler

et al. 2024

FEBS Open Bio

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The inner membrane of mitochondria contains hundreds of different integral membrane proteins. These proteins transport molecules into and out of the matrix, they carry out multifold catalytic reactions and they promote the biogenesis or degradation of mitochondrial constituents. Most inner membrane proteins are encoded by nuclear genes and synthesized in the cytosol from where they are imported into mitochondria by translocases in the outer and inner membrane. Three different import routes direct proteins into the inner membrane and allow them to acquire their appropriate membrane topology. First, mitochondrial import intermediates can be arrested at the level of the TIM23 inner membrane translocase by a stop‐transfer sequence to reach the inner membrane by lateral insertion. Second, proteins can be fully translocated through the TIM23 complex into the matrix from where they insert into the inner membrane in an export‐like reaction. Carriers and other polytopic membrane proteins embark on a third insertion pathway: these hydrophobic proteins employ the specialized TIM22 translocase to insert from the intermembrane space (IMS) into the inner membrane. This review article describes these three targeting routes and provides an overview of the machinery that promotes the topogenesis of mitochondrial inner membrane proteins.

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Novel Channels of the Outer Membrane of Mitochondria: Recent Discoveries Change Our View

Checchetto

Szabó

2018

BioEssays

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Ion channels mediate ion flux across biological membranes and regulate important organellar and cellular tasks. A recent study revealed the presence of four new proteins, the MIM complex (composed by Mim1 and Mim2), Ayr1, OMC7, and OMC8, that are able to form ion-conducting channels in the outer mitochondria membrane (OMM). These findings strongly indicate that the OMM is endowed with many solute-specific channels, in addition to porins and known channels mediating protein import into mitochondria. These solute-specific channels provide essential pathways for the controlled transport of ions and metabolites and may thus add a further layer of specificity to the regulation of mitochondrial function at the organelle-cytosol and/or inter-organellar interface. Future studies will be required to fully understand the way(s) of regulation of these new channels and to integrate them into signaling pathways within the cells.

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

Cited by 43 publications

References 89 publications

Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

Protein insertion into the inner membrane of mitochondria: routes and mechanisms

Novel Channels of the Outer Membrane of Mitochondria: Recent Discoveries Change Our View

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