The TRPM7 channel is inactivated by PIP(2) hydrolysis.
TRPM7 (ChaK1, TRP-PLIK, LTRPC7) is a ubiquitous, calcium-permeant ion channel that is unique in being both an ion channel and a serine/threonine kinase. The kinase domain of TRPM7 directly associates with the C2 domain of phospholipase C ( PLC). Here, we show that in native cardiac cells and heterologous expression systems, G alpha q- linked receptors or tyrosine kinase receptors that activate PLC potently inhibit channel activity. Numerous experimental approaches demonstrated that phosphatidylinositol 4,5-bisphosphate (PIP(2)), the substrate of PLC, is a key regulator of TRPM7. We conclude that receptor-mediated activation of PLC results in the hydrolysis of localized PIP(2), leading to inactivation of the TRPM7 channel.[1]References
- The TRPM7 channel is inactivated by PIP(2) hydrolysis. Runnels, L.W., Yue, L., Clapham, D.E. Nat. Cell Biol. (2002) [Pubmed]
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