Multiple Bcl-2 family members demonstrate selective dimerizations with Bax. | Zendy

Thomas W. Sedlak | Zendy; Zoltán N. Oltvai | Zendy; Elizabeth Yang | Zendy; Kai Wang | Zendy; Lawrence Boise | Zendy; Craig B. Thompson | Zendy; S J Korsmeyer | Zendy

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Multiple Bcl-2 family members demonstrate selective dimerizations with Bax.

Author(s) -

Thomas W. Sedlak,

Zoltán N. Oltvai,

Elizabeth Yang,

Kai Wang,

Lawrence Boise,

Craig B. Thompson,

S J Korsmeyer

Publication year - 1995

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.92.17.7834

Subject(s) - apoptosis , bcl 2 family , biology , programmed cell death , microbiology and biotechnology , yeast , bcl 2 associated x protein , chemistry , genetics , caspase 3

A family of Bcl-2-related proteins regulates cell death and shares highly conserved BH1 and BH2 domains. BH1 and BH2 domains of Bcl-2 were required for it to heterodimerize with Bax and to repress apoptosis. A yeast two-hybrid assay accurately reproduced this interaction and defined a selectivity and hierarchy of further dimerizations. Bax also heterodimerizes with Bcl-xL, Mcl-1, and A1. A Gly-159-->Ala substitution in BH1 of Bcl-xL disrupted its heterodimerization with Bax and abrogated its inhibition of apoptosis in mammalian cells. This suggests that the susceptibility to apoptosis is determined by multiple competing dimerizations in which Bax may be a common partner.

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