| Role of cysteine amino acid residues in calnexin. | |
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MedLine Citation:
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PMID: 21842374 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Calnexin is an endoplasmic reticulum protein that has a role in folding newly synthesized glycoproteins. In this study, we used site-specific mutagenesis to disrupt cysteine and histidine amino acid residues in the N- and P-domains of calnexin and determined whether these mutations impact the structure and function of calnexin. We identified that disruption of the N-domain cysteines resulted in significant loss of the chaperone activity of calnexin toward the glycosylated substrate, IgY, while disruption of the P-domain cysteines only had a small impact toward IgY. We observed that wild-type calnexin as well as the P-domain double cysteine mutant contained an intramolecular disulfide bond which is lost when the N-domain cysteines are mutated. Mutation to the N-domain histidine and N-domain cysteines resulted in increased binding of ERp57. Mutations to the P-domain cysteines further enhanced ERp57 binding to calnexin. Taken together, these observations indicated that the cysteine residues within calnexin were important for the structure and function of calnexin. |
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Authors:
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Helen Coe; Jeannine D Schneider; Monika Dabrowska; Jody Groenendyk; Joanna Jung; Marek Michalak |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-8-13 |
Journal Detail:
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Title: Molecular and cellular biochemistry Volume: - ISSN: 1573-4919 ISO Abbreviation: - Publication Date: 2011 Aug |
Date Detail:
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Created Date: 2011-8-15 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0364456 Medline TA: Mol Cell Biochem Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Departments of Pediatrics, School of Molecular and Systems Medicine, University of Alberta, Edmonton, AB, T6G 2H7, Canada. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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