Apoptosis: a balance between life and death? This review explores the BCL-2 protein family, key regulators of apoptosis. These proteins, sharing homology in conserved BH1-4 domains, control dimerization and influence apoptotic pathways. BCL-XL, BCL-2, and BAX can form ion-conductive pores in artificial membranes, suggesting a direct role in membrane permeability during cell death.
Composed of both pro-apoptotic and anti-apoptotic members, the BCL-2 family acts upstream of CASPASES and mitochondrial dysfunction, serving as a critical checkpoint in cell fate determination. BID and BAD, possessing the minimal death domain BH3, connect survival signals to the BCL-2 family, highlighting the integration of external cues in regulating apoptosis.
This comprehensive analysis reveals a reciprocal expression pattern of BCL-2 and BCL-XL during lymphocyte development, indicating stage-specific roles in immune cell maturation. This exploration provides insights into the intricate mechanisms governing cell death and survival, with implications for understanding and treating diseases involving dysregulated apoptosis.
This article, published in the Annual Review of Immunology, is directly relevant to the journal's focus on the molecular mechanisms of immune regulation. By reviewing the BCL-2 family and their role in apoptosis, the paper aligns with the journal's scope and contributes to understanding the cellular processes underlying immune responses.