Syntaxin 1A and receptor for activated C kinase interact with the N-terminal region of human dopamine transporter

Neurochem Res. 2004 Jul;29(7):1405-9. doi: 10.1023/b:nere.0000026404.08779.43.


The dopamine transporter (DAT) regulates the extent and duration of dopamine receptor activation through sodium-dependant reuptake of dopamine into presynaptic neurons, resulting in termination of dopaminergic neurotransmission. Using the yeast two-hybrid system, we have identified novel interactions between DAT, the SNARE protein syntaxin 1A, and the receptor for activated C kinases (RACK1). This association involves the intracellular N-terminal domain of human DAT (hDAT). Our data suggest that hDAT may exist as dimers or oligomers and that its protein-protein interactions with syntaxin 1A and RACK1 form functional regulatory complexes that may mediate DAT trafficking through modulation of hDAT phosphorylation by PKC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Surface / chemistry
  • Antigens, Surface / metabolism*
  • Binding Sites
  • Cloning, Molecular
  • Dopamine Plasma Membrane Transport Proteins
  • Humans
  • Membrane Glycoproteins*
  • Membrane Transport Proteins / chemistry*
  • Membrane Transport Proteins / metabolism*
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / metabolism*
  • Protein Kinase C / metabolism
  • Receptors for Activated C Kinase
  • Receptors, Cell Surface / chemistry
  • Receptors, Cell Surface / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / metabolism
  • Syntaxin 1


  • Antigens, Surface
  • Dopamine Plasma Membrane Transport Proteins
  • Membrane Glycoproteins
  • Membrane Transport Proteins
  • Nerve Tissue Proteins
  • Receptors for Activated C Kinase
  • Receptors, Cell Surface
  • Recombinant Proteins
  • SLC6A3 protein, human
  • STX1A protein, human
  • Syntaxin 1
  • Protein Kinase C