SUMOylation of Syntaxin1A regulates presynaptic endocytosis.
SUMOylation of Syntaxin1A regulates presynaptic endocytosis.
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DOI：
10.1038/srep17669
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发表时间：
2015-12-04
影响因子：
4.6
通讯作者：
Henley JM
中科院分区：
文献类型：
--
作者：
Craig TJ;Anderson D;Evans AJ;Girach F;Henley JM
突触前末梢的神经递质释放受到非常精确的空间和时间控制。神经递质释放后，突触小泡通过内吞作用进行回收并重新充满神经递质。在导致释放的胞吐作用过程中，SNARE 蛋白为膜融合提供大部分机械力。在这里，我们展示了其中一种蛋白质 Syntaxin1A，在其 C 端跨膜结构域附近以活性依赖性方式进行 SUMO 化。防止 Syntaxin1A 的 SUMO 化会减少其与其他 SNARE 蛋白的相互作用，并破坏突触小泡内吞/胞吐作用的平衡，导致内吞作用增加。这些结果表明 SUMO 化调节 Syntaxin1A 在囊泡内吞作用中的新兴作用，进而调节神经递质释放和突触功能。
Neurotransmitter release from the presynaptic terminal is under very precise spatial and temporal control. Following neurotransmitter release, synaptic vesicles are recycled by endocytosis and refilled with neurotransmitter. During the exocytosis event leading to release, SNARE proteins provide most of the mechanical force for membrane fusion. Here, we show one of these proteins, Syntaxin1A, is SUMOylated near its C-terminal transmembrane domain in an activity-dependent manner. Preventing SUMOylation of Syntaxin1A reduces its interaction with other SNARE proteins and disrupts the balance of synaptic vesicle endo/exocytosis, resulting in an increase in endocytosis. These results indicate that SUMOylation regulates the emerging role of Syntaxin1A in vesicle endocytosis, which in turn, modulates neurotransmitter release and synaptic function.