The molecular machinery for fast and slow neurosecretion
The molecular machinery for fast and slow neurosecretion
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DOI：
10.1016/0959-4388(94)90002-7
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发表时间：
1994-01-01
影响因子：
5.7
通讯作者：
Martin, Thomas F. J.
中科院分区：
文献类型：
--
作者：
Martin, Thomas F. J.
最近的研究表明，突触囊泡对接和融合的分子机制由三种肉毒杆菌/破伤风神经毒素底物（synaptobrevin, syntaxin, SNAP-25）组成，这些底物是组成分泌所需蛋白质的同源物。提出的调节胞外分泌的低亲和力Ca2+传感器仍有待确定，尽管最近对synaptotagmin的研究表明，它与其他蛋白质一起可能发挥这一作用。致密核颗粒的受调节肽分泌利用类似的机制进行对接/融合，最近的研究表明，这一途径涉及一个由更高亲和力的Ca2+传感器调节的对接前步骤。
Recent studies indicate that the molecular machinery for synaptic vesicle docking and fusion consists of a triad of botulinum/tetanus neurotoxin substrates (synaptobrevin, syntaxin, SNAP-25) that are homologues of proteins required for constitutive secretion. Proposed low-affinity Ca2+sensors that regulate exocytosis remain to be identified, although recent studies on synaptotagmin suggest that it, along with other proteins, could play this role. Regulated peptide secretion from dense-core granules has been found to utilize a similar machinery for docking/fusion, and recent studies indicate that this pathway involves a pre-docking step that is regulated by a higher affinity Ca2+sensor.