Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not Bcl-X(sub L)
Article Abstract:
A distant member of the Bcl-2 family, BAD, heterodimerizes with Bcl-X(sub L) or Bcl-2, neutralizing their protective effect and promoting cell death. Cells phosphorylated BAD on two serine residues embedded in 14-3-3 consensus binding sites in the presence of survival factor IL-3. Phosphorylated BAD isolated in the cytosol was bound to 14-3-3, with only the nonphosphorylated BAD heterodimerized with Bcl-X(sub L) at membrane sites to promote cell death. BAD's cell death promotion activity was enhanced further with the substitution of serine phosphorylation sites.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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Bad, a heterodimeric partner for Bcl-x(L) and Bcl-2, displaces Bax and promotes cell death
Article Abstract:
Lambda-expression cloning and yeast two-hybrid screening help identify the interacting protein Bad, which is homologous to Bcl-2 in the BH1 and BH2 regions. Bad exhibits increased binding, dimerization and death repressor activity reversal with Bcl-XL, but not with Bcl-2. Restoration of apoptosis depends on the level of Bax during the dimerization of Bad with Bcl-XL. The efficiency of repression of death by Bcl-2 or Bcl-XL depends on Bad levels in the competing dimerizations that determine the proneness of a cell to a death signal.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Cell death: critical control points
Article Abstract:
The requirement of an intact cell death pathway for successful embryonic development and maintenance of normal tissue homeostasis is studied. The benefits of identification of critical control points in the cell death pathway to therapy are discussed.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
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