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, complicating 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, J. P., Pemberton, J. M., Chi, X., & Andrews, D. W. (2016). Using Förster-resonance energy transfer to measure protein interactions between Bcl-2 family proteins on mitochondrial membranes. In Methods in Molecular Biology (Vol. 1419, pp. 197–212). Humana Press Inc. https://doi.org/10.1007/978-1-4939-3581-9_15
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