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• W1749320268 abstract "Human voltage-dependent anion channel-2 (hVDAC-2) functions primarily as the crucial anti-apoptotic protein in the outer mitochondrial membrane, and additionally as a gated bidirectional metabolite transporter. The N-terminal helix (NTH), involved in voltage sensing, bears an additional 11-residue extension (NTE) only in hVDAC-2. In this study, we assign a unique role for the NTE as influencing the chaperone-independent refolding kinetics and overall thermodynamic stability of hVDAC-2. Our electrophysiology data shows that the N-helix is crucial for channel activity, whereas NTE sensitizes this isoform to voltage gating. Additionally, hVDAC-2 possesses the highest cysteine content, possibly for regulating reactive oxygen species content. We identify interdependent contributions of the N-helix and cysteines to channel function, and the measured stability in micellar environments with differing physicochemical properties. The evolutionary demand for the NTE in the presence of cysteines clearly emerges from our biochemical and functional studies, providing insight into factors that functionally demarcate hVDAC-2 from the other VDACs." @default.
• W1749320268 created "2016-06-24" @default.
• W1749320268 creator A5031226525 @default.
• W1749320268 creator A5048159874 @default.
• W1749320268 date "2015-12-01" @default.
• W1749320268 modified "2023-09-27" @default.
• W1749320268 title "N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry" @default.
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• W1749320268 doi "https://doi.org/10.1074/jbc.m115.693978" @default.
• W1749320268 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4683249" @default.
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• W1749320268 hasPublicationYear "2015" @default.
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