To the knowledge of the 20GYGFG24 sequence stretch of type-1 VDAC: to understand why BCl-XL B4 domain peptides keep HeLa cells closed in hypotonic surroundings

Molecular Genetics and Metabolism
F P Thinnes

Abstract

Type-1 VDAC/porin, as a part of its voltage sensor, includes a GxxxG motif sequence that has been shown to work as an ATP-binding site. The motif has also been demonstrated to function as an aggregation/membrane perturbation sequence that opens VDAC in the plasmalemma of neuronal cells in experiment on apoptosis induction. Here it is discussed how type-1 VDAC channels at the cell surface of HeLa cells in hypotonic surroundings might be kept closed after pre-incubation with BCl-XL B4 domain peptides.

References

Jan 20, 1998·Die Naturwissenschaften·F P Thinnes, S Reymann
Mar 29, 2000·Proceedings of the National Academy of Sciences of the United States of America·S ShimizuY Tsujimoto
Oct 13, 2004·The Journal of General Physiology·Seiko F OkadaRichard C Boucher

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Citations

Feb 20, 2013·Molecular Genetics and Metabolism·Friedrich P Thinnes
Sep 25, 2012·Molecular Genetics and Metabolism·Friedrich P Thinnes, Gerhard Burckhardt

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