Transport rates of GABA transporters: regulation by the N-terminal domain and syntaxin 1A.
Plasma membrane GABA transporters participate in neural signaling through re-uptake of neurotransmitter. The domains of the transporter that mediate GABA translocation and regulate transport are not well understood. In the present experiments, the N-terminal cytoplasmic domain of the GABA transporter GAT1 regulated substrate transport rates. This domain directly interacted with ... syntaxin 1A, a SNARE protein involved in both neurotransmitter release and modulation of calcium channels and cystic fibrosis transmembrane regulator (CFTR) chloride channels. The interaction resulted in a decrease in transporter transport rates. These data demonstrate that intracellular domains of the GABA and protein-protein interactions regulate substrate translocation, and identify a direct link between the machinery involved in transmitter release and re-uptake.
Mesh Terms:
Animals, Antigens, Surface, Botulinum Toxins, Carrier Proteins, Cells, Cultured, Cricetinae, GABA Plasma Membrane Transport Proteins, Hippocampus, Membrane Potentials, Membrane Proteins, Membrane Transport Proteins, Nerve Tissue Proteins, Neurons, Oocytes, Organic Anion Transporters, Protein Structure, Tertiary, RNA, Messenger, Rats, Synaptic Membranes, Synaptic Transmission, Synaptic Vesicles, Syntaxin 1, Xenopus, gamma-Aminobutyric Acid
Animals, Antigens, Surface, Botulinum Toxins, Carrier Proteins, Cells, Cultured, Cricetinae, GABA Plasma Membrane Transport Proteins, Hippocampus, Membrane Potentials, Membrane Proteins, Membrane Transport Proteins, Nerve Tissue Proteins, Neurons, Oocytes, Organic Anion Transporters, Protein Structure, Tertiary, RNA, Messenger, Rats, Synaptic Membranes, Synaptic Transmission, Synaptic Vesicles, Syntaxin 1, Xenopus, gamma-Aminobutyric Acid
Nat. Neurosci.
Date: Oct. 01, 2000
PubMed ID: 11017172
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