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The **Bcl-2 protein family** is a group of structurally related proteins central to the regulation of apoptosis (programmed cell death), primarily through control of mitochondrial outer membrane permeabilization (MOMP). This family is comprised of both antiapoptotic members (such as Bcl-2, Bcl-XL, and Mcl-1), which block apoptosis and promote cell survival, and proapoptotic members—including effector proteins (Bax, Bak) and BH3-only proteins (BAD, BID, PUMA, NOXA)—which promote cell death by enabling mitochondrial membrane permeabilization and the release of apoptogenic factors such as cytochrome c. The intricate balance and interaction between these proteins determines the commitment to cell survival or death. Dysregulation of Bcl-2 family proteins is a hallmark of several diseases, especially various cancers, making them key therapeutic targets. Drugs called BH3 mimetics, such as venetoclax, have been developed to inhibit antiapoptotic members, thereby inducing apoptosis in cancer cells.
Inhibition of antiapoptotic Bcl-2 proteins (restores apoptosis in cancer cells); Disruption of Bcl-2 or Bcl-XL binding to proapoptotic members (BH3 mimetics)
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