Chapter title |
Using Förster-Resonance Energy Transfer to Measure Protein Interactions Between Bcl-2 Family Proteins on Mitochondrial Membranes
|
---|---|
Chapter number | 15 |
Book title |
Programmed Cell Death
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3581-9_15 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3579-6, 978-1-4939-3581-9
|
Authors |
Justin P. Pogmore, James M. Pemberton, Xiaoke Chi, David W. Andrews, Pogmore, Justin P., Pemberton, James M., Chi, Xiaoke, Andrews, David W. |
Abstract |
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. |
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