Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to
regulate Ca2+ store release-induced Ca2+ entry in endothelial
cells.  Dept. of Pharmacology (M/C 868) College of Medicine,
Univ. of Illinois; 835 South Wolcott Ave., Chicago, IL 60612,
USA. AJP Cell Physiology (Impact Factor: 3.71). 01/2009;
296(3):C403-13. DOI: 10.1152/ajpcell.00470.2008 Source: PubMed
ABSTRACT Caveolin-1 (Cav-1) regulates agonist-induced Ca(2+)
entry in endothelial cells; however, how Cav-1 regulates this
process is poorly understood. Here, we describe that Cav-1
scaffold domain (NH(2)-terminal residues 82-101; CSD) interacts
with transient receptor potential canonical channel 1 (TRPC1)
and inositol 1,4,5-trisphosphate receptor 3 (IP(3)R3) to
regulate Ca(2+) entry. We have shown previously that the TRPC1
COOH-terminal residues 781-789 bind to CSD. In the present
study, we show that the TRPC1 COOH-terminal residues 781-789
truncated (TRPC1-CDelta781-789) mutant expression abolished
Ca(2+) store release-induced Ca(2+) influx in hum