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, Solomon H. Snyder

Research output: Contribution to journalArticlepeer-review

166 Scopus citations


Many ion channels are regulated by lipids, 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 channels, 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 sequence. 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.

Original languageEnglish (US)
Pages (from-to)99-104
Number of pages6
Issue number7029
StatePublished - Mar 3 2005

All Science Journal Classification (ASJC) codes

  • General


Dive into the research topics of 'Phospholipase Cγ1 controls surface expression of TRPC3 through an intermolecular PH domain'. Together they form a unique fingerprint.

Cite this