Syntaxin 1A and Receptor for Activated C Kinase Interact with the N-Terminal Region of Human Dopamine Transporter
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- Lee, KH., Kim, MY., Kim, DH. et al. Neurochem Res (2004) 29: 1405. doi:10.1023/B:NERE.0000026404.08779.43
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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.