The TRPM7 channel is inactivated by PIP2 hydrolysis
Top Cited Papers
- 9 April 2002
- journal article
- Published by Springer Nature in Nature Cell Biology
- Vol. 4 (5), 329-336
- https://doi.org/10.1038/ncb781
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, 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.Keywords
This publication has 48 references indexed in Scilit:
- Visual transduction in DrosophilaNature, 2001
- The trp ion channel familyNature Reviews Neuroscience, 2001
- LTRPC7 is a Mg·ATP-regulated divalent cation channel required for cell viabilityNature, 2001
- TRP-PLIK, a Bifunctional Protein with Kinase and Ion Channel ActivitiesScience, 2001
- Melastatin Expression and Prognosis in Cutaneous Malignant MelanomaJournal of Clinical Oncology, 2001
- TRPγ, a Drosophila TRP–Related Subunit, Forms a Regulated Cation Channel with TRPLNeuron, 2000
- From worm to man: three subfamilies of TRP channelsTrends in Neurosciences, 2000
- The Drosophila Light-Activated Conductance Is Composed of the Two Channels TRP and TRPLCell, 1996
- Molecular characterization of the drosophila trp locus: A putative integral membrane protein required for phototransductionNeuron, 1989
- Isolation of a putative phospholipase c gene of drosophila, norpA, and its role in phototransductionCell, 1988