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Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers

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dc.contributor.author Rocheville, M. en_US
dc.contributor.author Lange, D. C. en_US
dc.contributor.author Kumar, U. en_US
dc.contributor.author Sasi, R. en_US
dc.contributor.author Patel, R. C. en_US
dc.contributor.author Patel, Y. C. en_US
dc.date.accessioned 2006-06-22T14:16:49Z
dc.date.available 2006-06-22T14:16:49Z
dc.date.issued 2000-03 en_US
dc.identifier.citation J Biol Chem 275, 7862-9 (2000) en_US
dc.identifier.uri http://hdl.handle.net/1807.1/182
dc.description This article is hosted on a website external to the CBCRA Open Access Archive. Selecting “View/Open” below will launch the full-text article in another browser window.
dc.description.abstract The existence of receptor dimers has been proposed for several G protein-coupled receptors. However, the question of whether G protein-coupled receptor dimers are necessary for activating or modulating normal receptor function is unclear. We address this question with somatostatin receptors (SSTRs) of which there are five distinct subtypes. By using transfected mutant and wild type receptors, as well as endogenous receptors, we provide pharmacological, biochemical, and physical evidence, based on fluorescence resonance energy transfer analysis, that activation by ligand induces SSTR dimerization, both homo- and heterodimerization with other members of the SSTR family, and that dimerization alters the functional properties of the receptor such as ligand binding affinity and agonist-induced receptor internalization and up-regulation. Double label confocal fluorescence microscopy showed that when SSTR1 and SSTR5 subtypes were coexpressed in Chinese hamster ovary-K1 cells and treated with agonist they underwent internalization and were colocalized in cytoplasmic vesicles. SSTR5 formed heterodimers with SSTR1 but not with SSTR4 suggesting that heterodimerization is a specific process that is restricted to some but not all receptor subtype combinations. Direct protein interaction between different members of the SSTR subfamily defines a new level of molecular cross-talk between subtypes of the SSTR and possibly related receptor families. en_US
dc.description.provenance Made available in DSpace on 2006-06-22T14:16:49Z (GMT). No. of bitstreams: 1 Rocheville.2000.7862.html: 413 bytes, checksum: e9c20330e33a8eccb8b6a0de7e00c488 (MD5) Previous issue date: 2000-03 en
dc.format.extent 413 bytes
dc.format.mimetype text/html
dc.language.iso en en_US
dc.publisher American Society for Biochemistry and Molecular Biology en_US
dc.relation.uri http://www.asbmb.org/ en_US
dc.title Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers en_US
dc.type Article en_US

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