BCL2like

BCL2like refers to a group of proteins within the BCL-2 family that share sequence similarity with the prototypical BCL2 protein and are primarily involved in regulating apoptosis, the programmed cell death process. Members of the BCL2-like subset are often anti-apoptotic and promote cell survival, though the family also includes pro-apoptotic proteins and BH3-only regulators that can tip the balance toward cell death.

Structurally, many BCL2-like proteins contain multiple BCL-2 homology (BH) domains, typically BH1 through BH4, and a C-terminal transmembrane region that anchors them to membranes such as the outer mitochondrial membrane or the endoplasmic reticulum. This membrane localization is important for controlling mitochondrial outer membrane permeabilization (MOMP), a decisive step in apoptosis.

Functionally, BCL2-like proteins inhibit apoptosis by binding and sequestering pro-apoptotic proteins such as BAX, BAK, and certain BH3-only members, thereby preventing cytochrome c release and caspase activation. The balance between anti-apoptotic BCL2-like members and pro-apoptotic partners determines cell fate in response to cellular stress, development, and immune signaling.

Clinical relevance is notable because dysregulation of BCL2-like proteins is linked to cancer and other diseases. Overexpression can enable cancer cells to survive chemotherapy, while loss of anti-apoptotic BCL2-like activity can contribute to degenerative conditions. Targeted therapies, including BH3 mimetics that inhibit anti-apoptotic BCL2-like proteins, are in use or development for cancer treatment.

See also: BCL-2 family, apoptosis, mitochondrial apoptosis, BH3 mimetics, BAX, BAK.