Differential regulation of phospholipase C-beta2 activity and membrane interaction by Galphaq, Gbeta1gamma2, and Rac2.

ABSTRACT: We combined fluorescence recovery after photobleaching (FRAP) beam-size analysis with biochemical assays to investigate the mechanisms of membrane recruitment and activation of phospholipase C-beta(2) (PLCbeta(2)) by G protein alpha(q) and betagamma dimers. We show that activation by alpha(q) and betagamma differ from activation by Rac2 and from each other. Stimulation by alpha(q) enhanced the plasma membrane association of PLCbeta(2), but not of PLCbeta(2)Delta, which lacks the alpha(q)-interacting region. Although alpha(q) resembled Rac2 in increasing the contribution of exchange to the FRAP of PLCbeta(2) and in enhancing its membrane association, the latter effect was weaker than with Rac2. Moreover, the membrane recruitment of PLCbeta(2) by alpha(q) occurred by enhancing PLCbeta(2) ass

SUBMITTER: Gutman O 

PROVIDER: S-EPMC2823533 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature