Work

Cotranslational folding and calnexin binding during glycoprotein synthesis.

Year: 1995

Type: article

Abstract: To analyze cotranslational folding of influenza hemagglutinin in the endoplasmic reticulum of live cells, we used short pulses of radiolabeling followed by immunoprecipitation and analysis with a two-dimensional SDS/polyacrylamide gel system which was nonreducing in the first dimension and reducing in the second. It separated nascent glycopolypeptides of different length and oxidation state. Evidence was obtained for cotranslational disulfide formation, generation of conformational epitopes, N-linked glycosylation, and oligosaccharide-dependent binding of calnexin, a membrane-bound chaperone that binds to incompletely folded glycoproteins via partially glucose-trimmed oligosaccharides. When glycosylation or oligosaccharide trimming was inhibited, the folding pathway was perturbed, suggesting a role for N-linked oligosaccharides and calnexin during translation of hemagglutinin.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.92.14.6229

Authors: W Chen, J Helenius, I Braakman, A Helenius

Institution: Yale University

Language: English

Topic: Endoplasmic Reticulum Stress and Disease

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences

Awards: PROTEIN FOLDING IN THE ENDOPLASMIC RETICULUM, G405682730, Membrane Traffic in Normal and Transformed Cells, G685538248