| http://purl.uniprot.org/citations/16099817 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16099817 | http://www.w3.org/2000/01/rdf-schema#comment | "The G protein-coupled receptor for PTH and PTH-related protein (PTH1R) signals via many intracellular pathways. The purpose of this work is to investigate a G protein binding site on an intracellular domain of the PTH1R. The carboxy-terminal, cytoplasmic tail of the PTH1R fused to glutathione-S-transferase interacts with Gi/o proteins in vitro. All three subunits of the heterotrimer interact with the receptor C-tail. Activation of the heterotrimeric complex with GTPgammaS has no effect on Gbetagamma interactions, but markedly disrupts binding of the Galphai/o subunits to the receptor tail, suggesting that direct Gbetagamma binding indirectly links Galpha subunits to this region of the receptor. Gbetagamma subunits alone bind the C-tail with an affinity that is comparable to the heterotrimeric G protein complex. G protein complexes consisting of Galphashis6-beta1gamma2 and Galphaqhis6-beta1gamma2 also interact with the PTH1R tail in vitro. The Gbetagamma interaction domain is located on the juxta-membrane region of the tail between amino acids 468 and 491. Mutations that disrupt Gbetagamma interactions block PTH signaling via phospholipase Cbeta/[Ca2+]i and MAPK and markedly reduce signaling via adenylyl cyclase/cAMP. Herein, we define a domain on the PTH1R that is capable of binding G protein heterotrimeric complexes via direct Gbetagamma interactions."xsd:string |
| http://purl.uniprot.org/citations/16099817 | http://purl.org/dc/terms/identifier | "doi:10.1210/me.2005-0169"xsd:string |
| http://purl.uniprot.org/citations/16099817 | http://purl.uniprot.org/core/author | "Smrcka A.V."xsd:string |
| http://purl.uniprot.org/citations/16099817 | http://purl.uniprot.org/core/author | "Divieti P."xsd:string |
| http://purl.uniprot.org/citations/16099817 | http://purl.uniprot.org/core/author | "Bonacci T.M."xsd:string |
| http://purl.uniprot.org/citations/16099817 | http://purl.uniprot.org/core/author | "Mahon M.J."xsd:string |
| http://purl.uniprot.org/citations/16099817 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16099817 | http://purl.uniprot.org/core/name | "Mol Endocrinol"xsd:string |
| http://purl.uniprot.org/citations/16099817 | http://purl.uniprot.org/core/pages | "136-146"xsd:string |
| http://purl.uniprot.org/citations/16099817 | http://purl.uniprot.org/core/title | "A docking site for G protein betagamma subunits on the parathyroid hormone 1 receptor supports signaling through multiple pathways."xsd:string |
| http://purl.uniprot.org/citations/16099817 | http://purl.uniprot.org/core/volume | "20"xsd:string |
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