InterPro domain: IPR037862

PLC-beta (PLCbeta) is regulated by heterotrimeric G protein-coupled receptors through their C2 domain and long C-terminal extension which forms an autoinhibitory helix. There are four isoforms: PLC-beta1-4. These isoforms mediate the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) to propagate signals for several physiological responses [ 1 , 2 ].

PLC-beta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, a C2 domain and a C-terminal PDZ. This entry represents the PH domain of PLC-beta. The PH domain of PLC-beta2 and PLC-beta3 plays a dual role, much like PLC-delta1, by binding to the plasma membrane, as well as the interaction site for the catalytic activator [ 3 ].

1. Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1). Biochim. Biophys. Acta 1517, 63-72
2. Membrane-induced allosteric control of phospholipase C-β isozymes. J. Biol. Chem. 289, 29545-57
3. Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Nat. Struct. Mol. Biol. 13, 1135-40