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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

Cell | Nov 15, 1996

http://www.ncbi.nlm.nih.gov/pubmed/8929531

Extracellular survival factors alter a cell's susceptibility to apoptosis, often through posttranslational mechanisms. However, no consistent relationship has been established between such survival signals and the BCL-2 family, where the balance of death agonists versus antagonists determines susceptibility. One distant member, BAD, heterodimerizes with BCL-X(L) or BCL-2, neutralizing their protective effect and promoting cell death. In the presence of survival factor IL-3, cells phosphorylated BAD on two serine residues embedded in 14-3-3 consensus binding sites. Only the nonphosphorylated BAD heterodimerized with BCL-X(L) at membrane sites to promote cell death. Phosphorylated BAD was sequestered in the cytosol bound to 14-3-3. Substitution of serine phosphorylation sites further enhanced BAD's death-promoting activity. The rapid phosphorylation of BAD following IL-3 connects a proximal survival signal with the BCL-2 family, modulating this checkpoint for apoptosis.

Pubmed ID: 8929531 RIS Download

Mesh terms: 14-3-3 Proteins | Amino Acid Sequence | Carrier Proteins | Cell Death | Cell Survival | Cytosol | Dimerization | Interleukin-3 | Membranes | Models, Biological | Molecular Sequence Data | Phosphorylation | Protein Binding | Proteins | Proto-Oncogene Proteins | Proto-Oncogene Proteins c-bcl-2 | Serine | Signal Transduction | Tyrosine 3-Monooxygenase | bcl-Associated Death Protein | bcl-X Protein

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