IPR037862
PLC-beta, PH domain
InterPro entry
Short name | PLC-beta_PH |
Description
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].
References
1.Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1). Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC. Biochim. Biophys. Acta 1517, 63-72, (2000). View articlePMID: 11118617
2.Membrane-induced allosteric control of phospholipase C-β isozymes. Charpentier TH, Waldo GL, Barrett MO, Huang W, Zhang Q, Harden TK, Sondek J. J. Biol. Chem. 289, 29545-57, (2014). View articlePMID: 25193662
3.Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J. Nat. Struct. Mol. Biol. 13, 1135-40, (2006). View articlePMID: 17115053
Cross References
ENZYME