BAD is a member of the BCL-2 family. BCL-2 family members are regulators of the programmed cell death pathways. BAD induces apoptosis by inhibiting antiapoptotic BCL-2-family members – BCL-x, Bcl-2, thereby allowing two other pro-apoptotic proteins, BAK and BAX, to aggregate and induce release of cytochrome c, followed by caspase activation and apoptosis. Proapoptotic activity of BAD is regulated through its phosphorylation. Only the nonphosphorylated BAD heterodimerized with BCL-xl or Bcl-2. Phosphorylated BAD is sequestered in the cytosol by binding to 14-3-3. Under certain stress conditions, BAD is activated by dephosphorylation.
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