BAD protein, or Bcl-2-associated death promoter, is a member of the Bcl-2 protein family that is involved in the regulation of apoptosis (cell death). It functions as a pro-apoptotic protein, promoting cell death when activated. BAD protein interacts with other Bcl-2 family members, such as Bcl-2 and Bcl-xL, to regulate the release of cytochrome c from the mitochondria, which is a crucial step in the apoptotic cascade. The activity of BAD protein is regulated by phosphorylation. When BAD is phosphorylated, it dissociates from Bcl-2 and Bcl-xL, losing its pro-apoptotic function. Conversely, when BAD is dephosphorylated, it binds to Bcl-2 and Bcl-xL, inhibiting their anti-apoptotic activity and promoting apoptosis. The phosphorylation of BAD protein is mediated by several kinases, including AKT (also known as protein kinase B). AKT phosphorylates BAD at specific sites, preventing its interaction with Bcl-2 and Bcl-xL and thus inhibiting apoptosis. This mechanism is important in promoting cell survival and proliferation in response to growth factors and other stimuli.
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