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tBid Undergoes Multiple Conformational Changes at...
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