Gα_q and the Phospholipase Cβ3 X-Y Linker Regulate Adsorption and Activity on Compressed Lipid Monolayers.

ABSTRACT: Phospholipase Cβ (PLCβ) enzymes are peripheral membrane proteins required for normal cardiovascular function. PLCβ hydrolyzes phosphatidylinositol 4,5-bisphosphate, producing second messengers that increase intracellular Ca²⁺ level and activate protein kinase C. Under basal conditions, PLCβ is autoinhibited by its C-terminal domains and by the X-Y linker, which contains a stretch of conserved acidic residues required for interfacial activation. Following stimulation of G protein-coupled receptors, the heterotrimeric G protein subunit Gα_q allosterically activates PLCβ and helps orient the activated complex at the membrane for efficient lipid hydrolysis. However, the molecular basis for how the PLCβ X-Y linker, its C-terminal domains, Gα_q, and the membrane co

SUBMITTER: Hudson BN 

PROVIDER: S-EPMC7885793 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature