Ontology highlight
ABSTRACT:
SUBMITTER: Charpentier TH
PROVIDER: S-EPMC4207972 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Charpentier Thomas H TH Waldo Gary L GL Barrett Matthew O MO Huang Weigang W Zhang Qisheng Q Harden T Kendall TK Sondek John J
The Journal of biological chemistry 20140905 43
All peripheral membrane proteins must negotiate unique constraints intrinsic to the biological interface of lipid bilayers and the cytosol. Phospholipase C-β (PLC-β) isozymes hydrolyze the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) to propagate diverse intracellular responses that underlie the physiological action of many hormones, neurotransmitters, and growth factors. PLC-β isozymes are autoinhibited, and several proteins, including Gαq, Gβγ, and Rac1, directly engage distinct ...[more]