Dissecting the functions of protein-protein interactions: caveolin as a promiscuous partner. Focus on "Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to regulate Ca2+ store release-induced Ca2+ entry in endothelial cells".
Hardin
C D
CD
Dept. of Nutrition and Exercise Physiology, Univ. of Missouri, 217 Gwynn Hall, Columbia, MO 65211, USA. hardinc@missouri.edu
Vallejo
J
J
D000818:Animals; D020013:Calcium Signaling; D051242:Caveolin 1 / Q000235:genetics / Q000378:metabolism*; D042783:Endothelial Cells / Q000378:metabolism*; D006801:Humans; D053496:Inositol 1,4,5-Trisphosphate Receptors / Q000378:metabolism*; D051379:Mice; D009154:Mutation; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping; D050052:TRPC Cation Channels / Q000235:genetics / Q000378:metabolism*; D013917:Thrombin / Q000378:metabolism; D013997:Time Factors
C495540:CAV1 protein, human; C495541:Cav1 protein, mouse; D051242:Caveolin 1; C506929:ITPR3 protein, human; D053496:Inositol 1,4,5-Trisphosphate Receptors; D050052:TRPC Cation Channels; C096351:transient receptor potential cation channel, subfamily C, member 1; D013917:Thrombin