Phospholipase Cγ1 controls surface expression of TRPC3 through an intermolecular PH domain

Damian B. van Rossum, Randen L. Patterson, Sumit Sharma, Roxanne K. Barrow, Michael Kornberg, Donald L. Gill and Solomon H. Snyder ()
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Damian B. van Rossum: Johns Hopkins University School of Medicine
Randen L. Patterson: The Pennsylvania State University
Sumit Sharma: Johns Hopkins University School of Medicine
Roxanne K. Barrow: Johns Hopkins University School of Medicine
Michael Kornberg: Johns Hopkins University School of Medicine
Donald L. Gill: University of Maryland School of Medicine
Solomon H. Snyder: Johns Hopkins University School of Medicine

Nature, 2005, vol. 434, issue 7029, 99-104

Abstract: Abstract Many ion channels are regulated by lipids1,2,3, but prominent motifs for lipid binding have not been identified in most ion channels. Recently, we reported that phospholipase Cγ1 (PLC-γ1) binds to and regulates TRPC3 channels4, components of agonist-induced Ca2+ entry into cells. This interaction requires a domain in PLC-γ1 that includes a partial pleckstrin homology (PH) domain—a consensus lipid-binding and protein-binding sequence5,6. We have developed a gestalt algorithm to detect hitherto ‘invisible’ PH and PH-like domains, and now report that the partial PH domain of PLC-γ1 interacts with a complementary partial PH-like domain in TRPC3 to elicit lipid binding and cell-surface expression of TRPC3. Our findings imply a far greater abundance of PH domains than previously appreciated, and suggest that intermolecular PH-like domains represent a widespread signalling mode.

Date: 2005
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DOI: 10.1038/nature03340

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