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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria.

In healthy cells the antiapoptotic protein Bcl-2 adopts a topology typical of tail-anchored proteins with only the hydrophobic carboxyl terminus inserted into the membrane, as shown by labeling cell lysates with a membrane-impermeant sulfhydryl-specific reagent. Induction of apoptosis in cells triggered a change in the conformation of Bcl-2 such that cysteine 158 near the base of helix 5 inserted into the lipid bilayer of both endoplasmic reticulum and mitochondria where it was protected from labeling. Addition of a peptide corresponding to the BH3 domain of the proapoptotic protein Bim to cell lysates triggered a similar conformational change in Bcl-2, demonstrating that preexisting, membrane-bound Bcl-2 proteins change topology.[1]

References

  1. During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria. Kim, P.K., Annis, M.G., Dlugosz, P.J., Leber, B., Andrews, D.W. Mol. Cell (2004) [Pubmed]
 
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