INTERACTION OF SYNAPTOTAGMIN WITH THE CYTOPLASMIC DOMAINS OF NEUREXINS
INTERACTION OF SYNAPTOTAGMIN WITH THE CYTOPLASMIC DOMAINS OF NEUREXINS
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DOI：
10.1016/0896-6273(93)90320-q
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发表时间：
1993-02-01
期刊：
影响因子：
16.2
通讯作者：
SUDHOF, TC
中科院分区：
文献类型：
--
作者：
HATA, Y;DAVLETOV, B;SUDHOF, TC
突触凝集素是突触囊泡内含的一种主要结合钙离子的膜蛋白，从牛脑中纯化后固定在Sepharose4B上。脑膜蛋白在固定化突触素上的亲和层析显示，α-和β-neurexins以不依赖于钙的方式与突触素结合。将谷胱甘肽S转移酶与3种不同的神经氨酸或对照蛋白的胞质结构域融合后，发现突触凝集素与神经尿毒素的胞质结构域发生了特异性的相互作用，但不与对照蛋白的胞质结构域发生特异性相互作用。这种相互作用依赖于一个高度保守的40个氨基酸序列，该序列构成了Neurexins的大部分细胞质尾巴。我们的数据表明，质膜蛋白(Neurexins)的细胞质结构域与亚细胞器特异的蛋白(Synaptopagmin)之间存在直接的相互作用。这种相互作用可能在神经末梢突触小泡的对接和靶向方面发挥重要作用。
Synaptotagmin, a major intrinsic membrane protein of synaptic vesicles that binds Ca2+, was purified from bovine brain and immobilized onto Sepharose 4B. Affinity chromatography of brain membrane proteins on immobilized synaptotagmin revealed binding of alpha- and beta-neurexins to synaptotagmin in a Ca2+-independent manner. Using a series of recombinant proteins in which glutathione S-transferase was fused to the cytoplasmic domains of three different neurexins or of control proteins, it was found that synaptotagmin specifically interacts with the cytoplasmic domains of neurexins but not of control proteins. This interaction is dependent on a highly conserved, 40 amino acid sequence that makes up most of the cytoplasmic tails of the neurexins. Our data suggest a direct interaction between the cytoplasmic domains of a plasma membrane protein (the neurexins) and a protein specific for a subcellular organelle (synaptotagmin). Such an interaction could have an important role in the docking and targeting of synaptic vesicles in the nerve terminal.