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.
Mesh Terms:
Animals, Carbachol, Cell Line, Cholinergic Agonists, Diglycerides, Heart, Humans, Hydrolysis, Ion Channels, Membrane Proteins, Models, Biological, Myocardium, Patch-Clamp Techniques, Phosphatidylinositol 4,5-Diphosphate, Protein Kinase C, Protein Kinases, Protein Structure, Tertiary, Rats, Receptor, Muscarinic M1, Receptors, Muscarinic, Recombinant Fusion Proteins, TRPM Cation Channels, Two-Hybrid System Techniques, Type C Phospholipases, Yeasts
Nat. Cell Biol.
Date: May. 01, 2002
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