| http://purl.uniprot.org/citations/12766172 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12766172 | http://www.w3.org/2000/01/rdf-schema#comment | "We tested the hypothesis that RhoA, a monomeric GTP-binding protein, induces association of inositol trisphosphate receptor (IP3R) with transient receptor potential channel (TRPC1), and thereby activates store depletion-induced Ca2+ entry in endothelial cells. We showed that RhoA upon activation with thrombin associated with both IP3R and TRPC1. Thrombin also induced translocation of a complex consisting of Rho, IP3R, and TRPC1 to the plasma membrane. IP3R and TRPC1 translocation and association required Rho activation because the response was not seen in C3 transferase (C3)-treated cells. Rho function inhibition using Rho dominant-negative mutant or C3 dampened Ca2+ entry regardless of whether Ca2+ stores were emptied by thrombin, thapsigargin, or inositol trisphosphate. Rho-induced association of IP3R with TRPC1 was dependent on actin filament polymerization because latrunculin (which inhibits actin polymerization) prevented both the association and Ca2+ entry. We also showed that thrombin produced a sustained Rho-dependent increase in cytosolic Ca2+ concentration [Ca2+]i in endothelial cells overexpressing TRPC1. We further showed that Rho-activated Ca2+ entry via TRPC1 is important in the mechanism of the thrombin-induced increase in endothelial permeability. In summary, Rho activation signals interaction of IP3R with TRPC1 at the plasma membrane of endothelial cells, and triggers Ca2+ entry following store depletion and the resultant increase in endothelial permeability."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m302401200"xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/author | "Paria B.C."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/author | "Holinstat M."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/author | "Malik A.B."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/author | "Mehta D."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/author | "Minshall R.D."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/author | "Voyno-Yasenetskaya T."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/author | "Ahmmed G.U."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/author | "Tiruppathi C."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/pages | "33492-33500"xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/title | "RhoA interaction with inositol 1,4,5-trisphosphate receptor and transient receptor potential channel-1 regulates Ca2+ entry. Role in signaling increased endothelial permeability."xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://purl.uniprot.org/core/volume | "278"xsd:string |
| http://purl.uniprot.org/citations/12766172 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12766172 |
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| http://purl.uniprot.org/uniprot/#_B4DJU3-mappedCitation-12766172 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12766172 |