The role of palmitoylation in directing dopamine D1 receptor internalization through selective endocytic routes

Biochem Biophys Res Commun. 2011 Feb 18;405(3):445-9. doi: 10.1016/j.bbrc.2011.01.050. Epub 2011 Jan 15.


We previously determined that D1 receptors can endocytose through caveolae, a subset of lipid rafts, in addition to internalization via a clathrin-dependent pathway. In this report, we investigated the potential role that palmitoylation might have on directing D1 receptor internalization through either a clathrin or caveolar-dependent route. Through whole cell binding analysis and sucrose gradient fractionation studies, we demonstrated that although palmitoylation of the D1 receptor was not required for agonist-independent localization to caveolae, agonist induced internalization kinetics of a de-palmitoylated D1 receptor were accelerated ∼8-fold in comparison to wild-type D1 receptor and were very similar to that observed for clathrin-dependent D1 receptor internalization. Additionally, inhibition of the clathrin mediated pathway led to significant attenuation in the extent of agonist induced internalization of the de-palmitoylated D1 receptor, suggesting the de-palmitoylated D1 receptor was directed to a clathrin-dependent internalization pathway. Taken together, these data suggest that palmitoylation may be involved in directing agonist-dependent D1 receptor internalization through selective endocytic routes.

Publication types

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

MeSH terms

  • Animals
  • COS Cells
  • Chlorocebus aethiops
  • Clathrin / antagonists & inhibitors
  • Clathrin / metabolism
  • Endocytosis*
  • Lipoylation / genetics
  • Receptors, Dopamine D1 / chemistry
  • Receptors, Dopamine D1 / genetics
  • Receptors, Dopamine D1 / metabolism*


  • Clathrin
  • Receptors, Dopamine D1