| Autor: |
Jeffery E; Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA., Peters LR, Raghavan M |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of biological chemistry [J Biol Chem] 2011 Jan 28; Vol. 286 (4), pp. 2402-15. Date of Electronic Publication: 2010 Nov 12. |
| DOI: |
10.1074/jbc.M110.180877 |
| Abstrakt: |
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: |
MEDLINE |
| Externí odkaz: |
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