Constitutive dimerization of human serotonin 5-HT4 receptors in living cells

Magali Berthouze, Mohammed Ayoub, Olivier Russo, Lucie Rivail, Sames Sicsic, Rodolphe Fischmeister, Isabelle Berque-Bestel, Ralf Jockers, Frank Lezoualc'h

Research output: Contribution to journalArticlepeer-review

60 Citations (Scopus)


Serotonin 5-HT4 receptor isoforms are G protein-coupled receptors (GPCRs) with distinct pharmacological properties and may represent a valuable target for the treatment of many human disorders. Here, we have explored the process of dimerization of human 5-HT4 receptor (h5-HT4R) by means of co-immunoprecipitation and bioluminescence resonance energy transfer (BRET). Constitutive h5-HT4(d)R dimer was observed in living cells and membrane preparation of CHO and HEK293 cells. 5-HT4R ligands did not influence the constitutive energy transfer of the h5-HT4(d)R splice variant in intact cells and isolated plasma membranes. In addition, we found that h5-HT4(d)R and h5-HT 4(g)R which structurally differ in the length of their C-terminal tails were able to form constitutive heterodimers independently of their activation state. Finally, we found that coexpression of h5-HT4R and β2-adrenergic receptor (β2AR) led to their heterodimerization. Given the large number of h5-HT4R isoforms which are coexpressed in a same tissue, our results points out the complexity by which this 5-HTR sub-type mediates its biological effects.

Original languageEnglish
Pages (from-to)2973-2980
Number of pages8
JournalFEBS Letters
Issue number14
Publication statusPublished - Jun 6 2005
Externally publishedYes


  • Bioluminescence
  • G protein-coupled receptors
  • Receptor dimerization
  • Resonance energy transfer
  • Serotonin
  • cAMP

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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