Molecular chaperones and the regulation of neurotransmitter exocytosis.
Molecular chaperones and the regulation of neurotransmitter exocytosis.
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DOI：
10.1016/s0006-2952(01)00648-7
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发表时间：
2001-07
影响因子：
5.8
通讯作者：
Konrad E. Zinsmaier;Peter Bronk
中科院分区：
文献类型：
--
作者：
Konrad E. Zinsmaier;Peter Bronk
调节神经递质的释放取决于导致胞吐和胞吞的重复循环的事件的精确序列。这些事件是介导的一系列分子之间的相互作用，囊泡，质膜和胞质蛋白。一个新兴的主题是，分子伴侣可以引导稳定或瞬时蛋白质复合物的顺序重组，以促进内吞和胞吐机制的时间和空间调节，并确保通过囊泡循环的矢量通道。分子伴侣，专门为一些底物，非常适合参与调节过程，需要一些分子的灵活性，重新排列构象或寡聚蛋白质结构。本文强调了三种分子伴侣系统在调节神经递质释放中的重要性：通过N-乙基马来酰亚胺敏感因子（NSF）和可溶性NSF附着蛋白（SNAP）调节可溶性NSF附着蛋白受体（SNARE）复合物，通过70 kDa热休克同源蛋白（Hsc 70）使网格蛋白包被的囊泡去包被，以及半胱氨酸串蛋白和Hsc 70对SNARE复合物相关蛋白相互作用的调节。
Regulated neurotransmitter release depends on a precise sequence of events that lead to repeated cycles of exocytosis and endocytosis. These events are mediated by a series of molecular interactions among vesicular, plasma membrane, and cytosolic proteins. An emerging theme has been that molecular chaperones may guide the sequential restructuring of stable or transient protein complexes to promote a temporal and spatial regulation of the endo- and exocytotic machinery and to ensure a vectorial passage through the vesicle cycle. Chaperones, specialized for a few substrates, are ideally suited to participate in regulatory processes that require some molecular dexterity to rearrange conformational or oligomeric protein structures. This article emphasizes the significance of three molecular chaperone systems in regulated neurotransmitter release: the regulation of soluble NSF attachment protein receptor (SNARE) complexes by N-ethylmaleimide-sensitive factor (NSF) and the soluble NSF attachment protein (SNAP), the uncoating of clathrin-coated vesicles by the 70 kDa heat-shock cognate protein (Hsc70), and the regulation of SNARE complex-associated protein interactions by cysteine-string protein and Hsc70.