Journal
MOLECULAR CELL
Volume 6, Issue 1, Pages 41-51Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(00)00006-X
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Funding
- NHLBI NIH HHS [HL 03601] Funding Source: Medline
- NICHD NIH HHS [NIHP30-HD18655, P01 HD 24926] Funding Source: Medline
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The Bcl-2 homology 3 (BH3) domain of prodeath Bcl-2 family members mediates their interaction with prosurvival Bcl-2 family members and promotes apoptosis, We report that survival factors trigger the phosphorylation of the proapoptotic Bcl-2 family member BAD at a site (Ser-155) within the BAD BH3 domain. When BAD is bound to prosurvival Bcl-2 family members, BAD Ser-155 phosphorylation requires the prior phosphorylation of Ser-136, which recruits 14-3-3 proteins that then function to increase the accessibility of Ser-155 to survival-promoting kinases, Ser-155 phosphorylation disrupts the binding of BAD to prosurvival Bcl-2 proteins and thereby promotes cell survival. These findings define a mechanism by which survival signals inactivate a proapoptotic Bcl-2 family member, and suggest a role for 14-3-3 proteins as cofactors that regulate sequential protein phosphorylation events.
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