Journal article
tBid Undergoes Multiple Conformational Changes at the Membrane Required for Bax Activation*
Abstract
Bid is a Bcl-2 family protein that promotes apoptosis by activating Bax and eliciting mitochondrial outer membrane permeabilization (MOMP). Full-length Bid is cleaved in response to apoptotic stimuli into two fragments, p7 and tBid (p15), that are held together by strong hydrophobic interactions until the complex binds to membranes. The detailed mechanism(s) of fragment separation including tBid binding to membranes and release of the p7 …
Authors
Shamas-Din A; Bindner S; Zhu W; Zaltsman Y; Campbell C; Gross A; Leber B; Andrews DW; Fradin C
Journal
Journal of Biological Chemistry, Vol. 288, No. 30, pp. 22111–22127
Publisher
Elsevier
Publication Date
July 2013
DOI
10.1074/jbc.m113.482109
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AnimalsApoptosisBH3 Interacting Domain Death Agonist ProteinCaspase 8Cell MembraneFluorescence Resonance Energy TransferHeLa CellsHumansKineticsLiposomesMiceMice, KnockoutMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial MembranesModels, BiologicalModels, MolecularMutationPermeabilityProtein BindingProtein ConformationTime Factorsbcl-2-Associated X Protein