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- Title
The TRPM7 channel is inactivated by PIP<sub>2</sub> hydrolysis.
- Authors
Runnels, Loren W.; Yue, Lixia; Clapham, David E.
- Abstract
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, Gαq-linked receptors or tyrosine kinase receptors that activate PLC potently inhibit channel activity. Numerous experimental approaches demonstrated that phosphatidylinositol 4,5-bisphosphate (PIP2), the substrate of PLC, is a key regulator of TRPM7. We conclude that receptor-mediated activation of PLC results in the hydrolysis of localized PIP2, leading to inactivation of the TRPM7 channel.
- Publication
Nature Cell Biology, 2002, Vol 4, Issue 5, p329
- ISSN
1465-7392
- Publication type
Academic Journal
- DOI
10.1038/ncb781