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EMBO reports 5, 1, 30–34 (2004)
doi:10.1038/sj.embor.7400052
Roles of G-protein-coupled receptor dimerization
From ontogeny to signalling regulation
Sonia Terrillon & Michel Bouvier
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Department of Biochemistry, Université de Montréal, C.P. 6128, succursale Centre-Ville, Montréal, Québec, Canada H3C 3J7
To whom correspondence should be addressed
Michel Bouvier Tel: +1 514 343 6372; Fax: +1 514 343 2210; michel.bouvier@umontreal.ca
Received 13 August 2003; Accepted 4 November 2003.
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Abstract
The classical idea that G-protein-coupled receptors (GPCRs) function as monomeric entities has been unsettled by the emerging concept of GPCR dimerization. Recent findings have indicated not only that many GPCRs exist as homodimers and heterodimers, but also that their oligomeric assembly could have important functional roles. Several studies have shown that dimerization occurs early after biosynthesis, suggesting that it has a primary role in receptor maturation. G-protein coupling, downstream signalling and regulatory processes such as internalization have also been shown to be influenced by the dimeric nature of the receptors. In addition to raising fundamental questions about GPCR function, the concept of dimerization could be important in the development and screening of drugs that act through this receptor class. In particular, the changes in ligand-binding and signalling properties that accompany heterodimerization could give rise to an unexpected pharmacological diversity that would need to be considered.
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