Redox-dependent gating of VDAC by mitoNEET
Copyright policy )Redox-dependent gating of VDAC by mitoNEET
SignificanceThis work demonstrates that the outer mitochondrial-anchored [2Fe-2S] mitoNEET is able to bind within the central cavity of the voltage-dependent anion channel (VDAC) and regulate its gating in a redox-dependent manner. These findings have implications for ferroptosis, apoptosis, and iron metabolism by linking VDAC function, mitoNEET, and the redox environment of the cell. Furthermore, these findings introduce a potential player to the many mechanisms that may alter VDAC’s governance in times of homeostasis or strife.
- Rice University United States
- University of California, San Diego United States
- University of Missouri United States
- University of California, San Francisco United States
- Center for Theoretical Biological Physics United States
Iron-Sulfur Proteins, 570, Protein Structure, Secondary, 2'-Disulfonic Acid, Protein Conformation, 1.1 Normal biological development and functioning, 4, Iron, 610, Apoptosis, Mitochondria, Liver, 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid, Mitochondrial Proteins, Underpinning research, direct coupling, Protein Interaction Mapping, Animals, Ferroptosis, Homeostasis, Humans, Sheep, Binding Sites, Voltage-Dependent Anion Channel 1, Biological Sciences, Recombinant Proteins, ferroptosis, Mitochondria, Oxygen, VDAC1, CISD1, Kinetics, Liver, 5.1 Pharmaceuticals, mitoNEET, Mitochondrial Membranes, 4'-Diisothiocyanostilbene-2, Biochemistry and Cell Biology, Generic health relevance, Development of treatments and therapeutic interventions, Protein Multimerization, Dimyristoylphosphatidylcholine, Oxidation-Reduction
Iron-Sulfur Proteins, 570, Protein Structure, Secondary, 2'-Disulfonic Acid, Protein Conformation, 1.1 Normal biological development and functioning, 4, Iron, 610, Apoptosis, Mitochondria, Liver, 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid, Mitochondrial Proteins, Underpinning research, direct coupling, Protein Interaction Mapping, Animals, Ferroptosis, Homeostasis, Humans, Sheep, Binding Sites, Voltage-Dependent Anion Channel 1, Biological Sciences, Recombinant Proteins, ferroptosis, Mitochondria, Oxygen, VDAC1, CISD1, Kinetics, Liver, 5.1 Pharmaceuticals, mitoNEET, Mitochondrial Membranes, 4'-Diisothiocyanostilbene-2, Biochemistry and Cell Biology, Generic health relevance, Development of treatments and therapeutic interventions, Protein Multimerization, Dimyristoylphosphatidylcholine, Oxidation-Reduction
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