Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.
Expressed in a wide variety of tissues.
Belongs to the Bcl-2 family.
Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.
Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation. Ser-75 is phosphorylated by AKT/PKB, protein kinase A and PIM2.
Mitochondrion outer membrane. Cytoplasm. Upon phosphorylation, locates to the cytoplasm.
Immunofluorescence analysis of Bad expression using ab97733 at 1/2000, followed by a FITC-conjugated secondary antibody.. Du145 Human prostate carcinoma cells were cultured without (A) or with (B) 1µM of the triphosphatase inhibitor thapsigargin (THG) for 12 hr.
THG induces Ca2+ release from internal stores which can promote apoptosis. BAD staining was located diffusely throughout the cytoplasm of untreated cells (A), and localized to the mitochondria in treated cells (B).