Modes of Calreticulin Recruitment to the Major Histocompatibility Complex Class I Assembly Pathway

被引:45
作者
Del Cid, Natasha [2 ]
Jeffery, Elise
Rizvi, Syed Monem
Stamper, Ericca
Peters, Larry Robert [2 ]
Brown, William Clay [3 ]
Provoda, Chester [4 ,5 ]
Raghavan, Malini [1 ]
机构
[1] Univ Michigan, Sch Med, Dept Microbiol & Immunol, Ann Arbor, MI 48109 USA
[2] Univ Michigan, Grad Program Immunol, Ann Arbor, MI 48109 USA
[3] Univ Michigan, Struct Biol Ctr, Ann Arbor, MI 48109 USA
[4] Univ Michigan, Ctr Drug Targeting, Ann Arbor, MI 48109 USA
[5] Univ Michigan, Dept Pharmaceut Sci, Ann Arbor, MI 48109 USA
关键词
MHC CLASS-I; PEPTIDE-LOADING COMPLEX; CHAPERONE CALRETICULIN; MOLECULAR CHAPERONE; MUTATIONAL ANALYSIS; LISTERIOLYSIN-O; REDOX ACTIVITY; ERP57; TAPASIN; CALNEXIN;
D O I
10.1074/jbc.M109.085407
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Major histocompatibility complex (MHC) class I molecules are ligands for T-cell receptors of CD8(+) T cells and inhibitory receptors of natural killer cells. Assembly of the heavy chain, light chain, and peptide components of MHC class I molecules occurs in the endoplasmic reticulum (ER). Specific assembly factors and generic ER chaperones, collectively called the MHC class I peptide loading complex (PLC), are required for MHC class I assembly. Calreticulin has an important role within the PLC and induces MHC class I cell surface expression, but the interactions and mechanisms involved are incompletely understood. We show that interactions with the thiol oxidoreductase ERp57 and substrate glycans are important for the recruitment of calreticulin into the PLC and for its functional activities in MHC class I assembly. The glycan and ERp57 binding sites of calreticulin contribute directly or indirectly to complexes between calreticulin and the MHC class I assembly factor tapasin and are important for maintaining steady-state levels of both tapasin and MHC class I heavy chains. A number of destabilizing conditions and mutations induce generic polypeptide binding sites on calreticulin and contribute to calreticulin-mediated suppression of misfolded protein aggregation in vitro. We show that generic polypeptide binding sites per se are insufficient for stable recruitment of calreticulin to PLC substrates in cells. However, such binding sites could contribute to substrate stabilization in a step that follows the glycan and ERp57-dependent recruitment of calreticulin to the PLC.
引用
收藏
页码:4520 / 4535
页数:16
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