Dissociation of the G protein βγ from the Gq-PLCβ complex partially attenuates PIP2 hydrolysis.

摘要: Phospholipase C β (PLCβ), which is activated by the Gq-family of heterotrimeric G proteins, hydrolyzes inner membrane lipid phosphatidylinositol-4,5-bisphosphate (PIP2), generating diacylglycerol (DAG) and inositol-1,4,5-triphosphate (IP3). Since Gq PLCβ regulate many crucial cellular processes have been identified as major disease drivers, activation termination signaling Gαq subunit extensively studied. Gq-coupled receptor induces intense transient PIP2 hydrolysis, subsequently recovers to a low-intensity steady-state equilibrium. However, molecular underpinnings this equilibrium remain unclear. Here, we explored influence crosstalk between Gi/o pathways on metabolism in living cells using single-cell optogenetic approaches spatially temporally constrain signaling. Our data suggest that Gβγ complex component highly efficient lipase GαqGTP-PLCβ-Gβγ. We found over time, dissociates from complex, leaving less GαqGTP-PLCβ allowing significant partial recovery levels. findings also indicate subtype Gγ fine-tunes activity Gq-PLCβ, expressing with higher plasma interaction show lower recovery. Given shows cell- tissue-specific expression, our existence distinct Gq-PLCβ paradigms. Furthermore, these results outline process likely safeguards excessive