The Polypeptide Binding Conformation of Calreticulin Facilitates Its Cell-surface Expression under Conditions of Endoplasmic Reticulum Stress
| Autor: | Larry Robert Peters, Malini Raghavan, Elise Jeffery |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Glycan
Thapsigargin Biology Endoplasmic Reticulum Peptide Mapping Biochemistry Cell Line Mice chemistry.chemical_compound S100 Calcium Binding Protein G Stress Physiological Catalytic Domain Calcium-binding protein MHC class I Animals Humans Enzyme Inhibitors Molecular Biology Antigen processing Endoplasmic reticulum Histocompatibility Antigens Class I Cell Biology Cell biology Protein Transport Gene Expression Regulation chemistry Calbindin 2 Mutation Protein Structure and Folding Unfolded Protein Response biology.protein Unfolded protein response Calcium Calreticulin Molecular Chaperones Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 286:2402-2415 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m110.180877 |
| Popis: | We define two classes of calreticulin mutants that retain glycan binding activity; those that display enhanced or reduced polypeptide-specific chaperone activity, due to conformational effects. Under normal conditions, neither set of mutants significantly impacts the ability of calreticulin to mediate assembly and trafficking of major histocompatibility complex class I molecules, which are calreticulin substrates. However, in cells treated with thapsigargin, which depletes endoplasmic reticulum calcium, major histocompatibility complex class I trafficking rates are accelerated coincident with calreticulin secretion, and detection of cell-surface calreticulin is dependent on its polypeptide binding conformations. Together, these findings identify a site on calreticulin that is an important determinant of the induction of its polypeptide binding conformation and demonstrate the relevance of the polypeptide binding conformations of calreticulin to endoplasmic reticulum stress-induced interactions. |
| Databáze: | OpenAIRE |
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