D5 dopamine receptor carboxyl tail involved in D5-D2 heteromer formation

Biochem Biophys Res Commun. 2013 Feb 15;431(3):586-9. doi: 10.1016/j.bbrc.2012.12.139. Epub 2013 Jan 11.


We have demonstrated that D(5) and D(2) dopamine receptors exist as heteromers in cells, and determined these receptor interact through amino acids in the cytoplasmic regions of each receptor. Specifically involved in heteromer formation we identified in the carboxyl tail of the D(5) receptor three adjacent glutamic acid residues, and in intracellular loop 3 of the D(2) receptor two adjacent arginine residues. Any pairing of these three D(5) receptor glutamic acids were sufficient for heteromer formation. These identified residues in D(5) and D(2) receptors are oppositely charged and likely interact by electrostatic interactions.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • Cytoplasm / metabolism
  • Humans
  • Molecular Sequence Data
  • Protein Multimerization
  • Receptors, Dopamine D2 / chemistry*
  • Receptors, Dopamine D2 / genetics
  • Receptors, Dopamine D5 / chemistry*
  • Receptors, Dopamine D5 / genetics


  • DRD5 protein, human
  • Receptors, Dopamine D2
  • Receptors, Dopamine D5