Abstract
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
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Research Support, Non-U.S. Gov't
MeSH terms
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Antigens, Surface / chemistry
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Antigens, Surface / metabolism*
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Binding Sites
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Cloning, Molecular
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Dopamine Plasma Membrane Transport Proteins
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Humans
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Membrane Glycoproteins*
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Membrane Transport Proteins / chemistry*
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Membrane Transport Proteins / metabolism*
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / metabolism*
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Protein Kinase C / metabolism
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Receptors for Activated C Kinase
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae / metabolism
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Syntaxin 1
Substances
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Antigens, Surface
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Dopamine Plasma Membrane Transport Proteins
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Membrane Glycoproteins
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Membrane Transport Proteins
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Nerve Tissue Proteins
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Receptors for Activated C Kinase
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Receptors, Cell Surface
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Recombinant Proteins
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SLC6A3 protein, human
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STX1A protein, human
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Syntaxin 1
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Protein Kinase C