In Vitro Mapping of Calnexin Interaction with Ribosomes.
From: Department of Surgery, McGill University, Montreal, PQ, Canada.
Biochemical and biophysical research communications
- Publish Date: Mar 2006
- ISSN: 0006-291X
- Volume: 341
- Issue: 1
- Pages: 39-44
- Medium: Print
- Language: English
- Citation (JAMA): Delom Frédéric, Chevet Eric, et al. In Vitro Mapping of Calnexin Interaction with Ribosomes.. Biochem. Biophys. Res. Commun. Mar 2006;341:39-44
Abstract
Calnexin is an endoplasmic reticulum (ER) resident type I integral membrane phosphoprotein. This protein is actively involved in the ER glycoprotein quality control through its luminal domain. In addition, although calnexin also interacts with membrane-bound ribosomes, the nature of this interaction remains poorly characterized. Herein, using in vitro approaches, we demonstrate that calnexin cytosolic domain directly interacts with, at least 5 ribosomal proteins. Furthermore, we characterize more specifically its interaction with the ribosomal protein L4 and that L4 binds to the 19 carboxy terminal amino acids of calnexin. We suggest that the direct interaction of calnexin with membrane-bound ribosomes may represent a regulatory mechanism for its lectin-like chaperone function.
Mesh Headings (Keywords): Binding Sites, Calnexin, Escherichia coli, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, Recombinant Proteins, Ribosomal Proteins, Ribosomes
Check for Full Text / PubMed Unique Identifier (PMID): 16414013
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