Structural highlights
Function
[PLCB2_HUMAN] The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Phospholipase C (PLC) isozymes are directly activated by heterotrimeric G proteins and Ras-like GTPases to hydrolyze phosphatidylinositol 4,5-bisphosphate into the second messengers diacylglycerol and inositol 1,4,5-trisphosphate. Although PLCs play central roles in myriad signaling cascades, the molecular details of their activation remain poorly understood. As described here, the crystal structure of PLC-beta2 illustrates occlusion of the active site by a loop separating the two halves of the catalytic TIM barrel. Removal of this insertion constitutively activates PLC-beta2 without ablating its capacity to be further stimulated by classical G protein modulators. Similar regulation occurs in other PLC members, and a general mechanism of interfacial activation at membranes is presented that provides a unifying framework for PLC activation by diverse stimuli.
General and versatile autoinhibition of PLC isozymes.,Hicks SN, Jezyk MR, Gershburg S, Seifert JP, Harden TK, Sondek J Mol Cell. 2008 Aug 8;31(3):383-94. PMID:18691970[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hicks SN, Jezyk MR, Gershburg S, Seifert JP, Harden TK, Sondek J. General and versatile autoinhibition of PLC isozymes. Mol Cell. 2008 Aug 8;31(3):383-94. PMID:18691970 doi:10.1016/j.molcel.2008.06.018
