Abstract
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.
Original language | English (US) |
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Pages (from-to) | 6879-6883 |
Number of pages | 5 |
Journal | Journal of Biological Chemistry |
Volume | 265 |
Issue number | 12 |
State | Published - 1990 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology