scholarly journals Glycogen synthase kinase 3-mediated voltage-dependent anion channel phosphorylation controls outer mitochondrial membrane permeability during lipid accumulation

Hepatology ◽  
2013 ◽  
Vol 57 (1) ◽  
pp. 93-102 ◽  
Author(s):  
Cecile Martel ◽  
Maya Allouche ◽  
Davide Degli Esposti ◽  
Elena Fanelli ◽  
Céline Boursier ◽  
...  
Keyword(s):  
Membrane Permeability ◽  
Lipid Accumulation ◽  
Mitochondrial Membrane ◽  
Glycogen Synthase ◽  
Anion Channel ◽  
Glycogen Synthase Kinase 3 ◽  
Outer Mitochondrial Membrane ◽  
Voltage Dependent Anion Channel ◽  
Mitochondrial Membrane Permeability ◽  
Voltage Dependent

scholarly journals Redox-dependent gating of VDAC by mitoNEET

2019 ◽  
Vol 116 (40) ◽  
pp. 19924-19929 ◽  
Author(s):  
Colin H. Lipper ◽  
Jason T. Stofleth ◽  
Fang Bai ◽  
Yang-Sung Sohn ◽  
Susmita Roy ◽  
...  
Keyword(s):  
Mitochondrial Membrane ◽  
Anion Channel ◽  
Fatty Acid Transport ◽  
Dependent Manner ◽  
Outer Mitochondrial Membrane ◽  
Voltage Dependent Anion Channel ◽  
Ros Homeostasis ◽  
Parkinson’S Diseases ◽  
Voltage Dependent

MitoNEET is an outer mitochondrial membrane protein essential for sensing and regulation of iron and reactive oxygen species (ROS) homeostasis. It is a key player in multiple human maladies including diabetes, cancer, neurodegeneration, and Parkinson’s diseases. In healthy cells, mitoNEET receives its clusters from the mitochondrion and transfers them to acceptor proteins in a process that could be altered by drugs or during illness. Here, we report that mitoNEET regulates the outer-mitochondrial membrane (OMM) protein voltage-dependent anion channel 1 (VDAC1). VDAC1 is a crucial player in the cross talk between the mitochondria and the cytosol. VDAC proteins function to regulate metabolites, ions, ROS, and fatty acid transport, as well as function as a “governator” sentry for the transport of metabolites and ions between the cytosol and the mitochondria. We find that the redox-sensitive [2Fe-2S] cluster protein mitoNEET gates VDAC1 when mitoNEET is oxidized. Addition of the VDAC inhibitor 4,4′-diisothiocyanatostilbene-2,2′-disulfonate (DIDS) prevents both mitoNEET binding in vitro and mitoNEET-dependent mitochondrial iron accumulation in situ. We find that the DIDS inhibitor does not alter the redox state of MitoNEET. Taken together, our data indicate that mitoNEET regulates VDAC in a redox-dependent manner in cells, closing the pore and likely disrupting VDAC’s flow of metabolites.

Human Genes Encoding the Voltage-Dependent Anion Channel (VDAC) of the Outer Mitochondrial Membrane: Mapping and Identification of Two New Isoforms

Genomics ◽  
1994 ◽  
Vol 20 (1) ◽  
pp. 62-67 ◽  
Author(s):  
Elizabeth Blachly-Dyson ◽  
Antonio Baldini ◽  
Michael Litt ◽  
Edward R.B. McCabe ◽  
Michael Forte
Keyword(s):  
Mitochondrial Membrane ◽  
Anion Channel ◽  
Outer Mitochondrial Membrane ◽  
Voltage Dependent Anion Channel ◽  
Human Genes ◽  
Voltage Dependent ◽  
Genes Encoding

scholarly journals Biogenesis of Porin of the Outer Mitochondrial Membrane Involves an Import Pathway via Receptors and the General Import Pore of the Tom Complex

2001 ◽  
Vol 152 (2) ◽  
pp. 289-300 ◽  
Author(s):  
Thomas Krimmer ◽  
Doron Rapaport ◽  
Michael T. Ryan ◽  
Chris Meisinger ◽  
C. Kenneth Kassenbrock ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Mitochondrial Membrane ◽  
Anion Channel ◽  
Mitochondrial Outer Membrane ◽  
Outer Mitochondrial Membrane ◽  
Voltage Dependent Anion Channel ◽  
Surface Receptors ◽  
Voltage Dependent ◽  
Surface Receptor

Porin, also termed the voltage-dependent anion channel, is the most abundant protein of the mitochondrial outer membrane. The process of import and assembly of the protein is known to be dependent on the surface receptor Tom20, but the requirement for other mitochondrial proteins remains controversial. We have used mitochondria from Neurospora crassa and Saccharomyces cerevisiae to analyze the import pathway of porin. Import of porin into isolated mitochondria in which the outer membrane has been opened is inhibited despite similar levels of Tom20 as in intact mitochondria. A matrix-destined precursor and the porin precursor compete for the same translocation sites in both normal mitochondria and mitochondria whose surface receptors have been removed, suggesting that both precursors utilize the general import pore. Using an assay established to monitor the assembly of in vitro–imported porin into preexisting porin complexes we have shown that besides Tom20, the biogenesis of porin depends on the central receptor Tom22, as well as Tom5 and Tom7 of the general import pore complex (translocase of the outer mitochondrial membrane [TOM] core complex). The characterization of two new mutant alleles of the essential pore protein Tom40 demonstrates that the import of porin also requires a functional Tom40. Moreover, the porin precursor can be cross-linked to Tom20, Tom22, and Tom40 on its import pathway. We conclude that import of porin does not proceed through the action of Tom20 alone, but requires an intact outer membrane and involves at least four more subunits of the TOM machinery, including the general import pore.

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