Substrates regulate -aminobutyric acid transporters in a syntaxin 1A-dependent manner
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چکیده
منابع مشابه
Syntaxin 1A Interacts with Multiple Exocytic Proteins to Regulate Neurotransmitter Release In Vivo
Biochemical studies suggest that syntaxin 1A participates in multiple protein-protein interactions in the synaptic terminal, but the in vivo significance of these interactions is poorly understood. We used a targeted mutagenesis approach to eliminate specific syntaxin binding interactions and demonstrate that Drosophila syntaxin 1A plays multiple regulatory roles in neurotransmission in vivo. S...
متن کاملSyntaxin 1A binds to the cytoplasmic C terminus of Kv2.1 to regulate channel gating and trafficking.
Voltage-gated K(+) (Kv) 2.1 is the dominant Kv channel that controls membrane repolarization in rat islet beta-cells and downstream insulin exocytosis. We recently showed that exocytotic SNARE protein SNAP-25 directly binds and modulates rat islet beta-cell Kv 2.1 channel protein at the cytoplasmic N terminus. We now show that SNARE protein syntaxin 1A (Syn-1A) binds and modulates rat islet bet...
متن کاملDopamine transporter/syntaxin 1A interactions regulate transporter channel activity and dopaminergic synaptic transmission.
The Caenorhabditis elegans (C. elegans) dopamine (DA) transporter (DAT-1) regulates DA signaling through efficient DA reuptake following synaptic release. In addition to its DA transport function, DAT-1 generates detectable DA-gated currents that may influence neuronal excitability. Previously, we provided evidence that single Cl-channel events underlie DAT-1 currents. In these studies, we iden...
متن کاملOpen form of syntaxin-1A is a more potent inhibitor than wild-type syntaxin-1A of Kv2.1 channels.
We have shown that SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) proteins not only participate directly in exocytosis, but also regulate the dominant membrane-repolarizing Kv channels (voltage-gated K+ channels), such as Kv2.1, in pancreatic beta-cells. In a recent report, we demonstrated that WT (wild-type) Syn-1A (syntaxin-1A) inhibits Kv2.1 channel tra...
متن کاملSyntaxin 1A regulates ENaC channel activity.
Na(+) entry across the apical membranes of many absorptive epithelia is determined by the number (N) and open probability (P(o)) of epithelial sodium channels (ENaC). Previous results showed that the H3 domain of syntaxin-1A (S1A) binds to ENaC to reduce N, supporting a role for S1A in the regulation of ENaC trafficking. The aim of this study was to determine whether S1A-induced reductions in E...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2002
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.082712899