FOLDING OF VSV G-PROTEIN - SEQUENTIAL INTERACTION WITH BIP AND CALNEXIN
FOLDING OF VSV G-PROTEIN - SEQUENTIAL INTERACTION WITH BIP AND CALNEXIN
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DOI：
10.1126/science.7939687
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发表时间：
1994-10-21
期刊：
影响因子：
56.9
通讯作者：
HELENIUS, A
中科院分区：
文献类型：
--
作者：
HAMMOND, C;HELENIUS, A
内质网 (ER) 含有促进哺乳动物细胞中蛋白质折叠的分子伴侣。使用生物合成标记来研究两种分子伴侣 BiP 和钙连接蛋白与水泡性口炎病毒 (VSV) 糖蛋白（G 蛋白）的相互作用。 G 蛋白与伴侣的免疫共沉淀表明 BiP 最大程度地结合 G 蛋白的早期折叠中间体，而钙连接蛋白在短暂滞后后结合更多折叠的分子。 Castanospermine 是 ER 葡萄糖苷酶的抑制剂，可阻断蛋白质与钙联蛋白的结合并抑制 G 蛋白折叠。与钙联蛋白的相互作用对于 G 蛋白的有效折叠和部分折叠形式的保留是必要的。
The endoplasmic reticulum (ER) contains molecular chaperones that facilitate the folding of proteins in mammalian cells. Biosynthetic labeling was used to study the interactions of two chaperones, BiP and calnexin, with vesicular stomatitis virus (VSV) glycoprotein (G protein). Coimmunoprecipitation of G protein with the chaperones showed that BiP bound maximally to early folding Intermediates of G protein, whereas calnexin bound after a short lag to more folded molecules. Castanospermine, an inhibitor of ER glucosidases, blocked the binding of proteins to calnexin and inhibited G protein folding. Interaction with calnexin was necessary for efficient folding of G protein and for retention of partially folded forms.