Apolipoprotein L2 (APOL2)

Apolipoprotein L2 is a cytoplasmic lipid-binding protein of 337 amino acids and 37.1 kDa, primarily localized to the cytosol, nucleoplasm, and nuclear bodies. It is a member of the primate-specific apolipoprotein L family, sharing a conserved four-helical core structure, as determined by crystallography and NMR. APOL2 harbors a BH3-like motif but does not function as a classical BH3-only pro-apoptotic protein; contrary to its paralogs, it does not independently induce apoptosis or autophagy nor modulate cell death induced by interferon-gamma or viral infection in current experimental systems. APOL2 may interact weakly with Bcl-2 proteins, suggesting a possible but minor role in autophagy regulation. Its gene expression has been linked to certain cancers (notably, upregulation in ovarian/peritoneal carcinoma) and genetic studies have implicated APOL2 variation in the risk for schizophrenia, pointing to functions beyond lipid metabolism in endothelial and neuronal tissues. Its overall biological function and disease relevance remain active areas of investigation.

Other names

ApoL-IIAPOL-IIApolipoprotein L-IIapolipoprotein L-IIAPOL3apolipoprotein L, 2apolipoprotein L2