SNARE蛋白如何打开融合孔？
How could SNARE proteins open a fusion pore?
作者信息
Fang Qinghua, Lindau Manfred
机构信息
School of Applied and Engineering Physics, Cornell University, Ithaca, New York; and Laboratory for Nanoscale Cell Biology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
School of Applied and Engineering Physics, Cornell University, Ithaca, New York; and Laboratory for Nanoscale Cell Biology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany
出版信息
Physiology (Bethesda). 2014 Jul;29(4):278-85. doi: 10.1152/physiol.00026.2013.
Abstract
The SNARE (Soluble NSF Attachment protein REceptor) complex, which in mammalian neurosecretory cells is composed of the proteins synaptobrevin 2 (also called VAMP2), syntaxin, and SNAP-25, plays a key role in vesicle fusion. In this review, we discuss the hypothesis that, in neurosecretory cells, fusion pore formation is directly accomplished by a conformational change in the SNARE complex via movement of the transmembrane domains.
摘要
SNARE（可溶性 NSF 附着蛋白受体）复合体在哺乳动物神经分泌细胞中由突触小泡蛋白 2（也称为 VAMP2）、 syntaxin 和 SNAP-25 组成，在囊泡融合中起关键作用。在本综述中，我们讨论了这样一种假说：在神经分泌细胞中，融合孔的形成是通过跨膜结构域的移动，由 SNARE 复合体的构象变化直接完成的。
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