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Tubulin-blocked state of VDAC studied by polymer and ATP partitioning.


ABSTRACT: Recently reported functional interaction between voltage-dependent anion channel of the outer mitochondrial membrane, VDAC, and dimeric tubulin is observed as a reversible channel blockage. Using partitioning of poly-(ethylene glycol)s of different molecular weights and reversal potential measurements, we probe the size and ion selectivity of the fully open and tubulin-blocked states of VDAC reconstituted into planar lipid bilayers. While the effective radius of the channel decreases by only a factor of 1.34±0.15, the selectivity reverses from initially anionic to cationic. Directly measuring ATP partitioning we demonstrate that these changes prohibit ATP from entering the channel in its tubulin-blocked state.

SUBMITTER: Gurnev PA 

PROVIDER: S-EPMC3157246 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Tubulin-blocked state of VDAC studied by polymer and ATP partitioning.

Gurnev Philip A PA   Rostovtseva Tatiana K TK   Bezrukov Sergey M SM  

FEBS letters 20110625 14


Recently reported functional interaction between voltage-dependent anion channel of the outer mitochondrial membrane, VDAC, and dimeric tubulin is observed as a reversible channel blockage. Using partitioning of poly-(ethylene glycol)s of different molecular weights and reversal potential measurements, we probe the size and ion selectivity of the fully open and tubulin-blocked states of VDAC reconstituted into planar lipid bilayers. While the effective radius of the channel decreases by only a f  ...[more]

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