CELLUBREVIN IS A UBIQUITOUS TETANUS-TOXIN SUBSTRATE HOMOLOGOUS TO A PUTATIVE SYNAPTIC VESICLE FUSION PROTEIN
CELLUBREVIN IS A UBIQUITOUS TETANUS-TOXIN SUBSTRATE HOMOLOGOUS TO A PUTATIVE SYNAPTIC VESICLE FUSION PROTEIN
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DOI：
10.1038/364346a0
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发表时间：
1993-07-22
期刊：
影响因子：
64.8
通讯作者：
SUDHOF, TC
中科院分区：
文献类型：
--
作者：
MCMAHON, HT;USHKARYOV, YA;SUDHOF, TC
破伤风毒素通过选择性阻断突触囊泡融合抑制神经递质释放1，2。最近，破伤风毒素显示出在体外和神经末梢中蛋白水解降解突触泡蛋白II（也称为VAMP-2），突触泡特异性蛋白3，4 5，6。作为破伤风毒素的靶蛋白，小突触素可能在突触小泡的胞吐融合中起作用。在这里，我们描述了一个新的synaptobrevin同系物，cellubrevin，这是目前在所有的细胞和组织测试，并证明它是一个膜运输蛋白的组成性回收途径。与小突触泡蛋白II一样，小突触泡蛋白在体外和转染后被破伤风毒素轻链蛋白水解。我们的研究结果表明，组成和调节囊泡途径使用同源蛋白膜贩运，可能是在质膜膜融合，表明这些途径之间的更大的机制和进化的相似性比以前认为的。
TETANUS toxin inhibits neurotransmitter release by selectively blocking fusion of synaptic vesicles1,2. Recently tetanus toxin was shown to proteolytically degrade synaptobrevin II (also named VAMP-2), a synaptic vesicle-specific protein3,4, in vitro and in nerve terminals5,6. As targets of tetanus toxin, synaptobrevins probably function in the exocytotic fusion of synaptic vesicles. Here we describe a new synaptobrevin homologue, cellubrevin, that is present in all cells and tissues tested and demonstrate that it is a membrane trafficking protein of a constitutively recycling pathway. Like synaptobrevin II, cellubrevin is proteolysed by tetanus toxin light chain in vitro and after transfection. Our results suggest that constitutive and regulated vesicular pathways use homologous proteins for membrane trafficking, probably for membrane fusion at the plasma membrane, indicating a greater mechanistic and evolutionary similarity between these pathways than previously thought.