Gating of the polycystin ion channel signaling complex in neurons and kidney cells.

Patrick Delmas, Surya M. Nauli, Xiaogang Li, Bertrand Coste, Nancy Osorio, Marcel Crest, David A. Brown, Jing Zhou

Research output: Contribution to journalArticlepeer-review

121 Scopus citations


Mutations in either polycystin-2 (PC2) or polycystin-1 (PC1) proteins cause severe, potentially lethal, kidney disorders and multiple extrarenal (including brain) disease phenotypes. PC2, a member of the transient receptor potential channel superfamily, and PC1, an orphan membrane receptor of largely unknown function, are thought to be part of a common signaling pathway. Here, we show that in rat sympathetic neurons and kidney cells, coassembly of full-length PC1 with PC2 forms a plasmalemmal ion channel signaling complex in which PC1 stimulation simultaneously activates PC2 ion channels and Gi/o-proteins. PC2 activation occurs through a structural rearrangement of PC1, independent of G-protein activation. Thus, PC1 acts as a prototypical membrane receptor that concordantly regulates PC2 channels and G-proteins, a bimodal mechanism that may account for the multifunctional roles of polycystin proteins in fundamental cellular processes of various cell types.

Original languageEnglish (US)
Pages (from-to)740-742
Number of pages3
JournalThe FASEB journal : official publication of the Federation of American Societies for Experimental Biology
Issue number6
StatePublished - Apr 2004

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics


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