The Bcl-2 family of proteins regulates the process of mitochondrial outer membrane permeabilization, causing the release of cytochrome c and committing a cell to apoptosis. The majority of the functional interactions between these proteins occur at, on, or within the mitochondrial outer membrane, complicat- ing structural studies of the proteins and complexes. As a result most in vitro studies of these protein- protein interactions use truncated proteins and/or detergents which can cause artificial interactions. Herein, we describe a detergent-free, fluorescence-based, in vitro technique to study binding between full-length recombinant Bcl-2 family proteins, particularly cleaved BID (cBID) and BCL-XL , on the membranes of purified mitochondria
CITATION STYLE
Pogmore, Justin., Pemberton, James., Chi, Xiaoke., & Andrews, David. (2016). Using FRET to measure protein interactions between Bcl-2 family proteins on mitochondrial membranes. Program Cell Death: Methods and Protocols in Molecular Biology, 1419, 197–212.
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