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首页> 外文期刊>Life sciences >CA2+/PHOSPHOLIPID-BINDING AND SYNTAXIN-BINDING OF NATIVE SYNAPTOTAGMIN I
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CA2+/PHOSPHOLIPID-BINDING AND SYNTAXIN-BINDING OF NATIVE SYNAPTOTAGMIN I

机译：天然突触素I的CA2 + /磷脂结合和sybinaxin结合

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Synaptotagmin, a synaptic vesicle protein endowed with multiple properties, is the putative calcium sensor in neuroexocytosis. Ca2+/phospholipid binding and syntaxin binding activity of synaptotagmin were previously investigated using recombinant fusion proteins. in phospholipid binding the EC50 for calcium obtained was different when fusion proteins containing one (C2A) or both (C2A+C2B) binding domains were used. it was alternatively proposed that one or both synaptotagmin binding domains are important for calcium-sensing and triggering of transmitter release. In this study the binding activity of native full-length synaptotagmin, immobilized on beads, was investigated. We found the kinetic parameters of Ca2+/phospholipid binding to be compatible with the role of calcium sensor for synaptotagmin (EC50 for calcium = 72 +/- 7 mu M), with the two C2 domains supporting separate and complementary calcium sensing properties. The binding of native syntaxin to synaptotagmin was measurable in the absence of calcium, but was markedly stimulated (2.2-fold) in the presence of mM calcium. It may be speculated that the two domains have a synergistic action in fast synchronous transmitter release, whereas C2B domain alone may support stow asynchronous release, working as a high affinity calcium sensor. [References: 28]
机译：Synaptotagmin是一种具有多种特性的突触小泡蛋白，是神经胞吐作用中公认的钙传感器。先前已使用重组融合蛋白研究了突触标签蛋白的Ca2 + /磷脂结合和语法素结合活性。在磷脂结合方面，当使用包含一个（C2A）或两个（C2A + C2B）结合域的融合蛋白时，获得的钙的EC50不同。或者，提出了一个或两个突触结合蛋白结合域对于钙敏感和触发递质释放是重要的。在这项研究中，研究了固定在珠子上的天然全长突触结合蛋白的结合活性。我们发现，Ca2 + /磷脂结合的动力学参数与突触标签素的钙传感器的作用（钙的EC50 = 72 +/- 7μM）兼容，两个C2域支持独立和互补的钙传感特性。在不存在钙的情况下可以测量天然语法素与突触结合蛋白的结合，但是在存在mM钙的情况下可以明显刺激（2.2倍）。可以推测，这两个域在快速同步发射器释放中具有协同作用，而单独的C2B域则可以支持储藏异步释放，充当高亲和力钙传感器。 [参考：28]

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