Functional significance of serotonin receptor dimerization
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Updated: May 10, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
1Center for Neuropharmacology and Neuroscience, Albany Medical College, Neil Hellman Medical Research Building, Mail code, 136, 47 New Scotland Ave., Albany, NY, 12208, USA, daviskh@mail.amc.edu.
Abstract:
The original model of G-protein activation by a single G-protein-coupled receptor (GPCR) is giving way to a new model, wherein two protomers of a GPCR dimer interact with a single G-protein. This article will review the evidence suggesting that 5-HT receptors form dimers/oligomers and will compare the findings with the results obtained from the studies with other biogenic amine receptors. Topics to be covered include the origin or biogenesis of dimer formation, potential dimer interface(s), and oligomer size (dimer vs. tetramer or higher order). The functional significance will be discussed in terms of G-protein activation following ligand binding to one or two protomers in a dimeric structure, the formation of heterodimers, and the development of bivalent ligands.
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