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Science 21 October 1994:
Vol. 266. no. 5184, pp. 456 - 458
DOI: 10.1126/science.7939687

Articles

Science, Vol 266, Issue 5184, 456-458
Copyright © 1994 by American Association for the Advancement of Science


articles

Folding of VSV G protein: sequential interaction with BiP and calnexin

C Hammond and A Helenius

Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.

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.


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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »
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   Full Text »    PDF »
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S. Kellokumpu, M. Suokas, L. Risteli, and R. Myllyla (1997)
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   Abstract »    Full Text »    PDF »
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M Ermonval, R Cacan, K Gorgas, I. Haas, A Verbert, and G Buttin (1997)
J. Cell Sci. 110, 323-336
   Abstract »    PDF »
A Soluble Secretory Reporter System in Trypanosoma brucei. STUDIES ON ENDOPLASMIC RETICULUM TARGETING.
J. D. Bangs, E. M. Brouch, D. M. Ransom, and J. L. Roggy (1996)
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   Abstract »    Full Text »    PDF »
Novel Covalent Chaperone Complexes Associated with Human Chorionic Gonadotropin beta Subunit Folding Intermediates.
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   Abstract »    Full Text »    PDF »
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Reduction of BiP Levels Decreases Heterologous Protein Secretion in Saccharomyces cerevisiae.
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Calnexin Fails to Associate with Substrate Proteins in Glucosidase-deficient Cell Lines.
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Chaperone Function of Calreticulin When Expressed in the Endoplasmic Reticulum as the Membrane-anchored and Soluble Forms.
I. Wada, S.-i. Imai, M. Kai, F. Sakane, and H. Kanoh (1995)
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Conformational Changes Induced in the Endoplasmic Reticulum Luminal Domain of Calnexin by Mg-ATP and Ca[IMAGE].
W.-J. Ou, J. J. M. Bergeron, Y. Li, C. Y. Kang, and D. Y. Thomas (1995)
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Role of the Endoplasmic Reticulum Chaperone Calnexin in Subunit Folding and Assembly of Nicotinic Acetylcholine Receptors.
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Transient Aggregation of Major Histocompatibility Complex Class II Chains during Assembly in Normal Spleen Cells.
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J. Biol. Chem. 270, 10475-10481
   Abstract »    Full Text »    PDF »
Glycosylation of Human Truncated Fc[IMAGE]RI alpha Chain Is Necessary for Efficient Folding in the Endoplasmic Reticulum.
O. Letourneur, S. Sechi, J. Willette-Brown, M. W. Robertson, and J.-P. Kinet (1995)
J. Biol. Chem. 270, 8249-8256
   Abstract »    Full Text »    PDF »
Calreticulin Functions as a Molecular Chaperone in the Biosynthesis of Myeloperoxidase.
W. M. Nauseef, S. J. McCormick, and R. A. Clark (1995)
J. Biol. Chem. 270, 4741-4747
   Abstract »    Full Text »    PDF »
Endoplasmic Reticulum (ER)-associated Degradation of Misfolded N-Linked Glycoproteins Is Suppressed upon Inhibition of ER Mannosidase I.
F. Tokunaga, C. Brostrom, T. Koide, and P. Arvan (2000)
J. Biol. Chem. 275, 40757-40764
   Abstract »    Full Text »    PDF »
BiP and PDI Cooperate in the Oxidative Folding of Antibodies in Vitro.
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   Abstract »    Full Text »    PDF »
Characterization of the Biosynthesis of Human Immunodeficiency Virus Type 1 Env from Infected T-cells and the Effects of Glucose Trimming of Env on Virion Infectivity.
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The Lectin Chaperone Calnexin Utilizes Polypeptide-based Interactions to Associate with Many of Its Substrates in Vivo.
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