Syntaphilin: A syntaxin-1 clamp that controls SNARE assembly

被引：82

作者：

Lao, GF

Scheuss, V

Gerwin, CM

Su, QN

Mochida, S

Rettig, J

Sheng, ZH ^{[1
]}

机构：

[1] NINDS, Synapt Funct Unit, NIH, Bethesda, MD 20892 USA

[2] Max Planck Inst Biophys Chem, Dept Membrane Biophys, D-37077 Gottingen, Germany

[3] Tokyo Med Univ, Dept Physiol, Tokyo 1608402, Japan

来源：

NEURON | 2000年 / 25卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0896-6273(00)80882-X

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

Syntaxin-1 is a key component of the synaptic vesicle docking/fusion machinery that forms the SNARE complex with VAMP/synaptobrevin and SNAP-25. Identifying proteins that modulate SNARE complex formation is critical for understanding the molecular mechanisms underlying neurotransmitter release and its modulation. We have cloned and characterized a protein called syntaphilin that is selectively expressed in brain. Syntaphilin competes with SNAP-25 for binding to syntaxin-1 and inhibits SNARE complex formation by absorbing free syntaxin-1. Transient overexpression of syntaphilin in cultured hippocampal neurons significantly reduces neurotransmitter release. Furthermore, introduction of syntaphilin into presynaptic superior cervical ganglion neurons in culture inhibits synaptic transmission. These findings suggest that syntaphilin may function as a molecular clamp that controls free syntaxin-1 availability for the assembly of the SNARE complex, and thereby regulates synaptic vesicle exocytosis.

引用

页码：191 / 201

页数：11

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[1] AN EVALUATION OF CAUSES FOR UNRELIABILITY OF SYNAPTIC TRANSMISSION [J].