Lewis M J, Pelham H R
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Cell. 1996 Apr 19;85(2):205-15. doi: 10.1016/s0092-8674(00)81097-1.
Operation of the secretory pathway in eukaryotic cells requires the selective docking and fusion of transport vesicles with the appropriate target organelle. This is mediated in part by integral membrane proteins termed v-SNAREs (on vesicles) and t-SNAREs (on the target membranes). We describe a novel yeast t-SNARE that resides on the endoplasmic reticulum and mediates retrograde traffic from the Golgi complex. Mutation of this protein prevents both the HDEL receptor and a membrane protein bearing a dibasic retrieval signal from recycling to the endoplasmic reticulum. Forward traffic is also blocked, but only indirectly. Comparison with other yeast mutants indicates that Sec21p (gamma-COP) and Sec20p (an endoplasmic reticulum membrane protein) are also involved primarily, if not exclusively, in retrograde transport.
真核细胞中分泌途径的运行需要运输小泡与合适的靶细胞器进行选择性对接和融合。这部分是由称为v-SNARE(位于小泡上)和t-SNARE(位于靶膜上)的整合膜蛋白介导的。我们描述了一种新的酵母t-SNARE,它位于内质网上,并介导从高尔基体复合体的逆行运输。该蛋白的突变阻止了HDEL受体和带有双碱性回收信号的膜蛋白循环回到内质网。顺行运输也被阻断,但只是间接的。与其他酵母突变体的比较表明,Sec21p(γ-COP)和Sec20p(一种内质网膜蛋白)也主要(如果不是唯一地)参与逆行运输。