title: 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.
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.
authors.forename: Friedrich P
authors.initials: FP
authors.lastname: Thinnes
mesh_terms: D000595:Amino Acid Sequence; D006367:HeLa Cells; D006801:Humans; D010455:Peptides / Q000737:chemistry; D054730:Protein Interaction Domains and Motifs; D050995:Voltage-Dependent Anion Channel 1 / Q000737:chemistry* / Q000235:genetics; D051020:bcl-X Protein / Q000737:chemistry
chemical_list: D010455:Peptides; C494762:VDAC1 protein, human; D051020:bcl-X Protein; D050995:Voltage-Dependent Anion Channel 1