Suppression of MHC class I surface expression by calreticulin's P-domain in a calreticulin deficient cell line

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1803, Issue 5, 2010, Pages 544-552

  Liu, Changzhen ^a   Fu, Hongmei ^b   Flutter, Barry ^b   Powis, Simon J ^c   Gao, Bin ^a,b  

^a INSTITUTE OF MICROBIOLOGY   (China)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

^c UNIVERSITY OF ST ANDREWS   (United Kingdom)

Author keywords

Calreticulin; MHC class I; P domain

Indexed keywords

CALRETICULIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

ANTIGEN PRESENTATION; ARTICLE; CELL LINE; CELL SURFACE; COMPLEX FORMATION; CONTROLLED STUDY; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEFECT; PROTEIN DOMAIN; PROTEIN EXPRESSION;

ANIMALS; ANTIGEN PRESENTATION; CALRETICULIN; CELLS, CULTURED; FIBROBLASTS; FLOW CYTOMETRY; FLUORESCENT ANTIBODY TECHNIQUE; HISTOCOMPATIBILITY ANTIGENS CLASS I; IMMUNOBLOTTING; IMMUNOPRECIPITATION; MICE; MICE, INBRED C57BL; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ANTIGEN, T-CELL; T-LYMPHOCYTES;

EID: 77951938419     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.03.001     Document Type: Article

References (37)

1. Cresswell P., Bangia N., Dick T., Diedrich G. The nature of the MHC class I peptide loading complex. Immunol. Rev. 1999, 172:21-28.
2. Helenius A., Trombetta E.S., Hebert D.N., Simons J.F. Calnexin, calreticulin and the folding of glycoproteins. Trends Cell Biol. 1997, 7:193-200.
3. Harris M.R., Yu Y.Y., Kindle C.S., Hansen T.H., Solheim J.C. Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I. J. Immunol. 1998, 160:5404-5409.
4. Sadasivan B., Lehner P.J., Ortmann B., Spies T., Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 1996, 5:103-114.
5. Solheim J.C., Carreno B.M., Hansen T.H. Are transporter associated with antigen processing (TAP) and tapasin class I MHC chaperones?. J. Immunol. 1997, 158:541-543.
6. Turnquist H.R., Vargas S.E., McIlhaney M.M., Li S., Wang P., Solheim J.C. Calreticulin binds to the alpha1 domain of MHC class I independently of tapasin. Tissue Antigens 2002, 59:18-24.
7. Harris M.R., Lybarger L., Yu Y.Y., Myers N.B., Hansen T.H. Association of 20 ERp57 with mouse MHC class I molecules is tapasin dependent and mimics that of calreticulin and not calnexin. J. Immunol. 2001, 166:6686-6692.
8. Elbein A.D. Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing. Faseb J. 1991, 5:3055-3063.
9. Gao B., Adhikari R., Howarth M., Nakamura K., Gold M.C., Hill A.B., Knee R., Michalak M., Elliott T. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 2002, 16:99-109.
10. Frickel E.M., Riek R., Jelesarov I., Helenius A., Wuthrich K., Ellgaard L. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:1954-1959.
11. Leach M.R., Cohen-Doyle M.F., Thomas D.Y., Williams D.B. Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J. Biol. Chem. 2002, 277:29686-29697.
12. Zapun A., Darby N.J., Tessier D.C., Michalak M., Bergeron J.J., Thomas D.Y. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 1998, 273:6009-6012.
13. Fu H., Liu C., Flutter B., Tao H., Gao B. Calreticulin maintains the low threshold of peptide required for efficient antigen presentation. Mol. Immunol. 2009, 46:3198-3206.
14. Howe C., Garstka M., Al-Balushi M., Ghanem E., Antoniou A., Fritzsche S., Jankevicius G., Kontouli1 N., Schneeweiss C., Williams A., Elliott T., Springer S. Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules. EMBO J. 2009, 28:3730-3744.
15. Helenius A., Aebi M. Intracellular functions of N-linked glycans. Science (New York, N.Y) 2001, 291:2364-2369.
16. Nauseef W.M., McCormick S.J., Clark R.A. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J. Biol. Chem. 1995, 270:4741-4747.
17. Peterson J.R., Ora A., Van P.N., Helenius A. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell 1995, 6:1173-1184.
18. Wada I., Imai S., Kai M., Sakane F., Kanoh H. Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms. J. Biol. Chem. 1995, 270:20298-20304.
19. Fruh K., Ahn K., Djaballah H., Sempe P., van Endert P.M., Tampe R., Peterson P.A., Yang Y. A viral inhibitor of peptide transporters for antigen presentation. Nature 1995, 375:415-418.
20. Lehner P.J., Karttunen J.T., Wilkinson G.W., Cresswell P. The human cytomegalovirus US6 glycoprotein inhibits transporter associated with antigen processing-dependent peptide translocation. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:6904-6909.
21. Neefjes J.J., Momburg F., Hammerling G.J. Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter. Science (New York, N.Y) 1993, 261:769-771.
22. Grandea A.G., Golovina T.N., Hamilton S.E., Sriram V., Spies T., Brutkiewicz R.R., Harty J.T., Eisenlohr L.C., Van Kaer L. Impaired assembly yet normal trafficking of MHC class I molecules in tapasin mutant mice. Immunity 2000, 13:213-222.
23. Karttunen J., Sanderson S., Shastri N. Detection of rare antigen-presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:6020-6024.
24. Sanderson S., Shastri N. LacZ inducible, antigen/MHC-specific T cell hybrids. Int. Immunol. 1994, 6:369-376.
25. Fu H., Ding J., Flutter B., Gao B. Investigation of endogenous antigen processing by delivery of an intact protein into cells. J. Immunol. Methods 2008, 335:90-97.
26. Lybarger L., Yu Y.Y., Chun T., Wang C.R., Grandea A.G., Van Kaer L., Hansen T.H. Tapasin enhances peptide-induced expression of H2-M3 molecules, but is not required for the retention of open conformers. J. Immunol. 2001, 167:2097-2105.
27. Vassilakos A., Michalak M., Lehrman M.A., Williams D.B. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 1998, 37:3480-3490.
28. David V., Hochstenbach F., Rajagopalan S., Brenner M.B. Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). J. Biol. Chem. 1993, 268:9585-9592.
29. Degen E., Cohen-Doyle M.F., Williams D.B. Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide. J. Exp. Med. 1992, 175:1653-1661.
30. Degen E., Williams D.B. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules. J. Cell Biol. 1991, 112:1099-1115.
31. Hochstenbach F., David V., Watkins S., Brenner M.B. Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:4734-4738.
32. Vassilakos A., Cohen-Doyle M.F., Peterson P.A., Jackson M.R., Williams D.B. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 1996, 15:1495-1506.
33. Moore S.E., Spiro R.G. Inhibition of glucose trimming by castanospermine results in rapid degradation of unassembled major histocompatibility complex class I 24 molecules. J. Biol. Chem. 1993, 268:3809-3812.
34. Antoniou A.N., Santos S.G., Campbell E.C., Lynch S., Arosa F.A., Powis S.J. ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove. FEBS Lett. 2007, 581:1988-1992.
35. Santos S.G., Campbell E.C., Lynch S., Wong V., Antoniou A.N., Powis S.J. Major histocompatibility complex class I-ERp57-tapasin interactions within the peptide-loading complex. J. Biol. Chem. 2007, 282:17587-17593.
36. Mesaeli N., Nakamura K., Zvaritch E., Dickie P., Dziak E., Krause K.H., Opas M., MacLennan D.H., Michalak M. Calreticulin is essential for cardiac development. J. Cell Biol. 1999, 144:857-868.
37. Nakamura K., Zuppini A., Arnaudeau S., Lynch J., Ahsan I., Krause R., Papp S., De Smedt H., Parys J.B., Muller-Esterl W., Lew D.P., Krause K.H., Demaurex N., Opas M., Michalak M. Functional specialization of calreticulin domains. J. Cell Biol. 2001, 154:961-972.