Evidence that membrane insertion of the cytosolic domain of Bcl-xL is governed by an electrostatic mechanism.

ABSTRACT: Signals from different cellular networks are integrated at the mitochondria in the regulation of apoptosis. This integration is controlled by the Bcl-2 proteins, many of which change localization from the cytosol to the mitochondrial outer membrane in this regulation. For Bcl-xL, this change in localization reflects the ability to undergo a conformational change from a solution to integral membrane conformation. To characterize this conformational change, structural and thermodynamic measurements were performed in the absence and presence of lipid vesicles with Bcl-xL. A pH-dependent model is proposed for the solution to membrane conformational change that consists of three stable conformations: a solution conformation, a conformation similar to the solution conformation but anchored to th

SUBMITTER: Thuduppathy GR 

PROVIDER: S-EPMC1785297 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature