Work

Glycan-dependent and -independent Association of Vesicular Stomatitis Virus G Protein with Calnexin

Year: 1996

Type: article

Abstract: Calnexin (CNX) is a membrane-bound molecular chaperone that associates with newly synthesized proteins in the endoplasmic reticulum. Although several studies have indicated that it interacts exclusively with glycoproteins that carry monoglucosylated N-linked oligosaccharides, others have reported that it can bind to proteins that have no glycans. To address this discrepancy, we translated wild-type vesicular stomatitis virus G protein and nonglycosylated mutant forms in the presence of microsomes and examined their association with CNX. Individual G protein molecules were found to efficiently associate with CNX when both glycans were present and less efficiently if there was only a single glycan. Nonglycosylated G protein also interacted with CNX, but only when misfolded and present in high molecular weight aggregates. The results indicated that CNX can interact with G protein in two ways: through an oligosaccharide-dependent mechanism that involves individual substrate proteins; and in an oligosaccharide-independent association with large aggregates.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.271.24.14280

Authors: Kurt S. Cannon, Daniel N. Hebert, Ari Helenius

Institution: Yale University

Language: English

Topic: Endoplasmic Reticulum Stress and Disease

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430