Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein.
Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein.
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DOI：
10.1016/s0021-9258(19)39231-2
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发表时间：
1990-04
期刊：
影响因子：
--
通讯作者：
Robert;-W.;DomsIlII;John;-K.;Rose
中科院分区：
文献类型：
--
作者：
Robert;-W.;DomsIlII;John;-K.;Rose
为了研究重链结合蛋白（BiP，GRP 78）在内质网中的功能，我们已经表征了其与模型质膜糖蛋白，水泡性口炎病毒的G蛋白的相互作用。我们使用了一组充分表征的突变G蛋白和抗BiP抗体的免疫沉淀，以确定BiP是否与新合成的G蛋白和/或保留在内质网中的突变G蛋白相互作用。我们进行了三个主要观察：1）BiP瞬时结合不完全二硫键的野生型G蛋白折叠中间体; 2）BiP不稳定结合所有留在内质网中的突变G蛋白; 3）BiP仅稳定结合不形成正确链内二硫键的突变G蛋白。
To investigate the function of heavy chain binding protein (BiP, GRP 78) in the endoplasmic reticulum, we have characterized its interaction with a model plasma membrane glycoprotein, the G protein of vesicular stomatitis virus. We used a panel of well characterized mutant G proteins and immunoprecipitation with anti-BiP antibodies to determine if BiP interacted with newly synthesized G protein and/or mutant G proteins retained in the endoplasmic reticulum. We made three major observations: 1) BiP bound transiently to folding intermediates of wild-type G protein which were incompletely disulfide-bonded; 2) BiP did not bind stably to all mutant G proteins which remain in the endoplasmic reticulum; and 3) BiP bound stably only to mutant G proteins which do not form correct intrachain disulfide bonds.