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The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein
Author(s) -
Holden Marcia J.,
Colombini Marco
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81040-8
Subject(s) - voltage dependent anion channel , bacterial outer membrane , biophysics , chemistry , porin , transmembrane protein , translocase of the outer membrane , translocase of the inner membrane , mitochondrial membrane transport protein , membrane potential , gating , mitochondrion , microbiology and biotechnology , inner mitochondrial membrane , biochemistry , biology , receptor , escherichia coli , gene
The mitochondrial outer membrane channel, VDAC, serves as the primary permeability pathway for metabolite flux between cytoplasmic and mitochondrial compartments. VDAC can occupy several conformational states differing in ion conductivity. Small transmembrane potentials cause transitions from open‐ to closed‐channel conformations. A soluble mitochondrial protein enhances the channel's response to voltage by increasing the rate of channel closing; inducing the occupation of lower conductance states; and decreasing the rate of channel reopening. This protein modulator acts at very low concentrations and its role in the cell may be to regulate the permeability of the mitochondrial outer membrane by inducing channel closure.