PRIMARY STRUCTURE AND ALTERNATIVE SPLICE VARIANTS OF GEPHYRIN, A PUTATIVE GLYCINE RECEPTOR TUBULIN LINKER PROTEIN
PRIMARY STRUCTURE AND ALTERNATIVE SPLICE VARIANTS OF GEPHYRIN, A PUTATIVE GLYCINE RECEPTOR TUBULIN LINKER PROTEIN
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DOI：
10.1016/0896-6273(92)90136-2
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发表时间：
1992-06-01
期刊：
影响因子：
16.2
通讯作者：
BETZ, H
中科院分区：
文献类型：
--
作者：
PRIOR, P;SCHMITT, B;BETZ, H
一种与哺乳动物抑制性甘氨酸受体（GlyR）相关的93 kd多肽定位于中枢突触，并与聚合小管蛋白具有高亲和力。这种蛋白质被命名为gephyrin（来自希腊语γ -epsilon-phi-upsilon-rho-alpha，桥），被认为是将GlyR固定在亚突触微管上。在这里，我们报告了从cDNA推断出的初级结构，并表明在所有检查的大鼠组织中都发现了相应的转录本。在大脑中，至少有五种不同的卟啉mrna是通过选择性剪接产生的。293肾细胞中gephyrin cdna的表达产生与gephyrin特异性抗体反应的多肽，其与聚合的微管蛋白共沉淀。因此，gephyrin可能定义了一种参与膜蛋白-细胞骨架相互作用的新型微管相关蛋白。
A 93 kd polypeptide associated with the mammalian inhibitory glycine receptor (GlyR) is localized at central synapses and binds with high affinity to polymerized tubulin. This protein, named gephyrin (from the Greek gamma-epsilon-phi-upsilon-rho-alpha, bridge), is thought to anchor the GlyR to subsynaptic microtubules. Here we report its primary structure deduced from cDNA and show that corresponding transcripts are found in all rat tissues examined. In brain, at least five different gephyrin mRNAs are generated by alternative splicing. Expression of gephyrin cDNAs in 293 kidney cells yields polypeptides reactive with a gephyrin-specific antibody, which coprecipitate with polymerized tubulin. Thus, gephyrin may define a novel type of microtubule-associated protein involved in membrane protein-cytoskeleton interactions.