Identification of Ser/Thr phosphorylation sites in the C2-domain of phospholipase C γ2 (PLCγ2) using TRPM7-kinase.

ABSTRACT: PLC-isozymes are central elements of cellular signaling downstream of numerous receptors. PLCγ2 is a pivotal component of B cell receptor (BCR) signaling. The regulation of PLCγ2-dependent signaling functions by Tyr-phosphorylation is well characterized, however, the potential role of Ser/Thr phosphorylation events remains undefined. TRPM7 is the fusion of a Ser/Thr kinase with an ion channel, and an essential component of Mg(2+)-homeostasis regulation. Although the interaction between the C2 domain of several PLC-isozymes and TRPM7 is well established, previous studies have focused on the effect of PLC-activity on TRPM7. Here, we investigated whether Ser/Thr phosphorylation sites in the C2 domain of PLCγ2 could be identified using TRPM7-kinase. We show that TRPM7-kinase phosphorylates PLC

SUBMITTER: Deason-Towne F 

PROVIDER: S-EPMC4049354 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature