In situ cleavage of the acidic domain from the p115 tether inhibits exocytic transport
In situ cleavage of the acidic domain from the p115 tether inhibits exocytic transport
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DOI：
10.1111/j.1600-0854.2008.00783.x
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发表时间：
2008-09-01
期刊：
影响因子：
4.5
通讯作者：
Warren, Graham
中科院分区：
文献类型：
--
作者：
Satoh, Ayano;Warren, Graham
高尔基体是一种卷曲螺旋蛋白，参与高尔基体的结构和功能。一个复合体的golgins（p115，GM 130和giantin），连同rab 1鸟苷三磷酸酶和顺式高尔基体SNARE，有助于介导融合过程中的入口面的高尔基体。p115的C-末端酸性结构域特异性结合GM 130和Giantin。然而，当使用RNA干扰消除/拯救方法时，体内该结构域的缺失似乎对胞吐转运没有影响（Puthenveedu MA，Linstedt AD.基因置换揭示了p115/SNARE相互作用对高尔基体的生物发生是必不可少的。Proc Natl Acad Sci U S A 2004;101：1253-1256）。在这项研究中，我们已经使用了不同的方法引入烟草蚀纹病毒（tev）蛋白酶切割位点到p115，使C-末端结构域可以快速，特异性地释放在体内通过显微注射的tev蛋白酶。结果表明，切割抑制了细胞外运输到细胞表面。
Golgins are coiled-coil proteins involved in Golgi architecture and function. A complex of golgins (p115, GM130 and giantin), together with the rab1 guanosine triphosphatase and cis Golgi SNAREs, helps to mediate fusion processes at the entry face of the Golgi apparatus. The C-terminal acidic domain of p115 binds specifically to GM130 and giantin. However, deletion of this domain in vivo appears to have no effect on exocytic transport when using an RNA interference depletion/rescue approach (Puthenveedu MA, Linstedt AD. Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis. Proc Natl Acad Sci U S A 2004;101:1253-1256). In this study, we have used a different approach introducing a tobacco etch virus (tev) protease cleavage site into p115 so that the C-terminal domain can be rapidly and specifically released in vivo by microinjection of the tev protease. The results show that cleavage inhibits exocytic transport to the cell surface.