Phospholipase C beta-3 (PLCB3)

Phospholipase C beta-3 (PLCB3) is an enzyme that plays a central role in signal transduction by hydrolyzing phosphatidylinositol 4,5-bisphosphate (PIP2) to generate the intracellular signaling messengers diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3)[3][7]. PLCB3 is a key effector of G protein–coupled receptor (GPCR) signaling, activated by Gαq/11 and Gβγ subunits and regulated through multiple protein interactions, phosphorylation events, and dimerization[1][4]. Its activity mediates diverse cellular responses, including the regulation of intracellular calcium release, activation of protein kinase C, actin cytoskeleton remodeling, chemotaxis in immune cells, and cell proliferation. PLCB3 is involved in physiological functions across multiple tissues, from immune cell activation and chemotaxis to smooth muscle contraction and epithelial ion transport. Dysregulation of PLCB3 has been linked to inflammatory diseases, cancer, certain leukemias, and rare genetic disorders such as spondylometaphyseal dysplasia with corneal dystrophy[1][2][7].

Other names

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3PLC-beta-3Phosphoinositide phospholipase C-beta-3SMDCDphospholipase C, beta 3 (phosphatidylinositol-specific)PLC beta 3

Catalytic hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) to generate the second messengers diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), leading to activation of PKC and calcium-dependent signaling[1][3][7]. Integrates signals from multiple pathways (e.g., oxytocin, cAMP/PKA, PKC) via phosphorylation and protein-protein interactions[1]. Regulation via complex formation with partners (e.g., GPCRs, calmodulin, ORP4L, NHERF1)[1][4].