首页> 外文期刊>Neuron >Syntaxin 1A interacts with multiple exocytic proteins to regulate neurotransmitter release in vivo.
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Syntaxin 1A interacts with multiple exocytic proteins to regulate neurotransmitter release in vivo.

机译:Syntaxin 1A与多种胞外蛋白相互作用,以调节体内神经递质的释放。

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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. Syntaxin mutations that eliminate ROP/Munc-18 binding display increased neurotransmitter release, suggesting that ROP inhibits neurosecretion through its interaction with syntaxin. Syntaxin mutations that block Ca2+ channel binding also cause an increase in neurotransmitter release, suggesting that syntaxin normally functions in inhibiting Ca2+ channel opening. Additionally, we identify and characterize a syntaxin Ca2+ effector domain, which may spatially organize the Ca2+ channel, cysteine string protein, and synaptotagmin for effective excitation-secretion coupling in the presynaptic terminal.
机译:生化研究表明,syntaxin 1A参与突触末端的多种蛋白质-蛋白质相互作用,但对这些相互作用的体内意义了解甚少。我们使用靶向诱变方法消除特定的syntaxin结合相互作用,并证明果蝇syntaxin 1A在体内神经传递中起多种调节作用。消除ROP / Munc-18结合的突触素突变体显示神经递质的释放增加,表明ROP通过与语法素的相互作用抑制神经分泌。阻滞Ca2 +通道结合的语法突变也引起神经递质释放的增加,这表明语法素通常在抑制Ca2 +通道开放中起作用。此外,我们识别并表征Ca2 +效应子域中的语法,它可以在空间上组织Ca2 +通道,半胱氨酸串蛋白和突触标记素,以在突触前末端有效激发-分泌偶联。

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