The COOH terminus of synaptotagmin mediates interaction with the neurexins.
The COOH terminus of synaptotagmin mediates interaction with the neurexins.
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DOI：
10.1016/s0021-9258(17)37233-2
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发表时间：
1994-03
期刊：
影响因子：
--
通讯作者：
M. Perin
中科院分区：
文献类型：
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作者：
M. Perin
突触囊泡蛋白（synaptotagmin）和突触前α-latrotoxin受体（neurexin）的相互作用被认为参与了突触囊泡在活性位点的对接或神经递质释放的调节。在这里，我报告的调查负责这种相互作用的synaptotagmin域。含有羧基末端的突触结合蛋白片段能够从溶解的脑匀浆中纯化neurexins。与COOH末端34个氨基酸对应的合成肽一样小的片段能够富集neurexins 100倍。neurexins与synaptotagmin的结合不依赖于钙离子，且具有中等亲和力。这突触结合蛋白的COOH-末端片段是保守的，在所有物种的特点，到目前为止。反映这一点，一个合成肽对应的果蝇synaptotagmin的羧基末端是能够纯化大鼠neurexins，这表明这种相互作用的可能性，也可能存在于果蝇。我建议，突触结合蛋白的羧基末端结合的neurexins的羧基末端，这种相互作用可能介导对接的突触囊泡或调制的神经递质释放。
The interaction of the synaptic vesicle protein, synaptotagmin, and the presynaptic alpha-latrotoxin receptor, a neurexin, has been proposed to be involved in docking of synaptic vesicles at active sites or modulation of neurotransmitter release. Here I report the investigation of the domain of synaptotagmin responsible for this interaction. Pieces of synaptotagmin containing the carboxyl terminus are capable of purifying neurexins from solubilized brain homogenates. Pieces as small as a synthesized peptide corresponding to the COOH-terminal 34 amino acids are capable of enriching neurexins 100-fold. The binding of neurexins to synaptotagmin is calcium-independent and of moderate affinity. This COOH-terminal segment of synaptotagmin is conserved in all species characterized to date. Reflective of this, a synthetic peptide corresponding to the carboxyl terminus of Drosophila synaptotagmin is capable of purification of rat neurexins, suggesting the possibility that this interaction may also exist in Drosophila. I propose that the carboxyl terminus of synaptotagmin binds to the carboxyl terminus of the neurexins and that this interaction may mediate docking of synaptic vesicles or modulation of neurotransmitter release.