Protein kinase C and casein kinase substrate in neurons protein 2 (PACSIN2)

Protein kinase C and casein kinase substrate in neurons protein 2 (PACSIN2) is a cytoplasmic F-BAR domain protein involved in sculpting membrane curvature and linking the actin cytoskeleton with vesicle formation through regulation of tubulin polymerization[2][5][6][7]. It is crucial for the formation and endocytosis of caveolae, small invaginations in the plasma membrane, by binding phospholipids and generating membrane tubules[2][6]. PACSIN2 interacts with several partners, including other PACSIN family members and elements of endocytic and cytoskeletal machinery, and is functionally important in processes like endothelial migration, angiogenesis, and cell polarity. Indirectly, it affects drug metabolism—its genetic variants influence thiopurine response and toxicity, making it a biomarker but not a current therapeutic target[3][5][7]. Additionally, PACSIN2 is implicated in disease contexts including infection, intestinal and kidney homeostasis, angiogenesis, and pharmacogenetics, but it is not a recognized direct therapeutic target.

Other names

SdpIISDPIISyndapin-2Syndapin-IIsyndapin IIprotein kinase C and casein kinase substrate in neurons protein 2cytoplasmic phosphoprotein PACSIN2syndapin2

No known drugs directly target PACSIN2. The functional impact is observed via genetic polymorphisms (notably rs2413739) that influence responses/toxicity to thiopurines such as mercaptopurine and methotrexate[3].