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Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers.

Jeong, SY; Gaume, B; Lee, YJ; Hsu, YT; Ryu, SW; Yoon, SH; Youle, RJ
The EMBO journal, 23(10):2146-2155, 2004
Journal Title
The EMBO journal
Bcl-x(L) is a potent inhibitor of apoptosis. While Bcl-x(L) can be bound to mitochondria, a substantial fraction, depending on the cell type or tissue, is found in the cytosol of healthy cells. Gel filtration and crosslinking experiments reveal that, unlike monomeric Bax, Bcl-x(L) migrates in a complex of approximately 50 kDa in the cytosol. Co-immunoprecipitation experiments indicate that Bcl-x(L) in the cytosol forms homodimers. The C-terminal hydrophobic tails of two Bcl-x(L) molecules are involved in homodimer formation, and analysis of mutants demonstrates that the C-terminal lysine residue and the G138 residue lining the BH3-binding pocket are required for homodimerization. The flexible loop preceding the C-terminal tail in Bcl-x(L) is longer than that of several monomeric Bcl-2 family members and is a requisite for the homodimer formation. Bad binding to Bcl-x(L) dissociates the homodimers and triggers Bcl-x(L) binding to mitochondrial membranes. The C-terminal tail of Bcl-x(L) is also required to mediate Bcl-x(L)/Bax heterodimer formation. Both mitochondrial import and antiapoptotic activity of different Bcl-x(L) mutants correlate with their ability to form homodimers.
MeSH terms
Amino Acid SequenceAnimalsApoptosis/physiologyBinding SitesCarrier Proteins/metabolismCell LineCytoplasm/metabolismDimerizationHumansMitochondria/metabolismMolecular Sequence DataMutationPeptide Fragments/genetics/metabolismProtein Binding*Protein Structure, Quaternary*Protein Structure, SecondaryProto-Oncogene Proteins/genetics/metabolismProto-Oncogene Proteins c-bcl-2/*chemistry/genetics/metabolismSequence Alignmentbcl-2-Associated X Proteinbcl-Associated Death Proteinbcl-X Protein
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