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- W2017490220 abstract "Bcl-2 family of proteins plays differential roles in regulation of mitochondria-mediated apoptosis, by either promoting or inhibiting the release of apoptogenic molecules from mitochondria to cytosol. Bcl-2 family proteins modulate the mitochondrial permeability through interaction with adenine nucleotide translocator (ANT), voltage-dependent anion channel (VDAC), ADP/ATP exchange, or oxidative phosphorylation during apoptosis. Although the mitochondrial homeostasis is affected by the relative ratio of pro- and anti-apoptotic Bcl-2 family members, the molecular mechanism underlying the release of mitochondrial intermembrane proteins remains elusive. Here we reported the biochemical evidence that both pro-apoptotic Bax and anti-apoptotic Bcl-X(L) might simultaneously contact the putative loop regions of human VDAC1, and the existence of VDAC1-Bax-Bcl-X(L) tertiary complex in vitro suggested that VDAC1 channel conformation and mitochondrial permeability could be determined by the delicate balance between Bax and Bcl-X(L)." @default.
- W2017490220 created "2016-06-24" @default.
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- W2017490220 date "2003-06-01" @default.
- W2017490220 modified "2023-10-02" @default.
- W2017490220 title "Identification of the protein–protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins" @default.
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- W2017490220 doi "https://doi.org/10.1016/s0006-291x(03)00871-4" @default.
- W2017490220 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12767928" @default.
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