The nature of the MHC class I peptide loading complex

Immunological Reviews

Volumn 172, Issue , 1999, Pages 21-28

  Cresswell, Peter ^a   Bangia, Naveen ^a   Dick, Tobias ^a   Diedrich, Gundo ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 MICROGLOBULIN; CALRETICULIN; CHAPERONE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MEMBRANE PROTEIN; OXIDOREDUCTASE; PROTEIN SUBUNIT;

COMPLEX FORMATION; ENDOPLASMIC RETICULUM; HOUSEKEEPING GENE; HUMAN; HUMAN CELL; MAJOR HISTOCOMPATIBILITY COMPLEX; PRIORITY JOURNAL; PROTEIN ASSEMBLY; REVIEW;

EID: 0033404775     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-065X.1999.tb01353.x     Document Type: Review

References (52)

1. 1. Hammond C, Helenius C. Quality control in the secretory pathway. Curr Opin Cell Biol 1995;7:523-529.
2. 2. Kopito RR. ER quality control: the cytoplasmic connection. Cell 1997;88:427-430.
3. 3. Morrison SL, Scharff MD. Heavy chain-producing variants of a mouse myeloma cell line. J Immunol 1975;114:655-659.
4. 4. Dulis BH, Kloppel TM, Grey HM, Kubo RT. Regulation of catabolism of IgM heavy chains in a B lymphoma cell line. J Biol Chem 1982;257:4369-4374.
5. 5. Bole DG, Hendershot LM, Kearney JF. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J Cell Biol 1986;102:1558-1566.
6. 6. Baumal R, Scharff MD. Synthesis, assembly and secretion of γ-globulin by mouse myeloma cells. V. Balanced and unbalanced synthesis of heavy and light chains by IgG-producing tumors and cell lines. J Immunol 1973;111:448-456.
7. 7. Dul JL, Aviel S, Melnick J, Argon Y. Ig light chains are secreted predominantly as monomers. J Immunol 1996;57:2969-2975.
8. 8. Lietzgen K, Knittler MR, Haas IG. Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding. J Biol Chem 1997;272:3117-3123.
9. 9. Hughes EA, Hammond C, Cresswell P. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc Natl Acad Sci USA 1997;94:1896-1901.
10. 10. Wiertz EJHJ, et al. Sec61 -mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 1996;384:432-438.
11. 11. Noessner E, Parham P. Species-specific differences in chaperone interaction of human and mouse histocompatibility complex class I molecules. J Exp Med 1995;181:327-337.
12. 12. Degen E, Cohen-Doyle MF, Williams DB. Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both β2-microglobulin and peptide. J Exp Med 1992;175:1653-61.
13. 13. Hochstenbach F, David V, Watkins S, Brenner MB. Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T-cell and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Proc Natl Acad Sci USA 1992;89:4734-4738.
14. 14. Jackson MR, Cohen-Doyle MF, Peterson PA, Williams DB. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science 1994;263:384.
15. 15. David V, Hochstenbach F, Rajagopalan S, Brenner MB. 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.
16. 2-microglobulin complexes associate with TAP transporters before peptide binding. Nature 1994;368:864-867.
17. 17. Vassilakos A, Cohen-Doyle MF, Peterson PA, Jackson MR, Williams DB. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J 1996;15:1495-1506.
18. 18. Sousa MC, Ferrero-Garcia MA, Parodi AJ. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc: glycoprotein glucosyltransferase. Biochemistry 1992;31:97-105.
19. 19. Trombetta SE, Parodi AJ. Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose: glycoprotein glucosyltransferase. J Biol Chem 1992;267:9236-9240.
20. 20. Degen E, Williams DB. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules. J Cell Biol 1991;112:1099-1115.
21. 21. Sadasivan B, Lehner PJ, 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.
22. 22. Van Leeuwen JEM, Kearse KP. Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes. Proc Natl Acad Sci USA 1996;93:13997-14001.
23. 23. Hughes EA, Cresswell P. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Curr Biol 1998;8:709-712.
24. 24. Morrice NA, Powis SJ. A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules. Curr Biol 1998;8:713-716.
25. 25. Lindquist JA, Jensen ON, Mann M, Hammerling GJ. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J 1998;17:2186-2195.
26. 26. Oliver JD, Van der Wal FJ, Bulleid NJ, High S. Interaction of the thiol-dependent reductase ERp57 with nascant glycoproteins. Science 1997;275:86-88.
27. 27. Elliott JG, Oliver JD, High S. The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J Biol Chem 1997;272:13849-13855.
28. 28. Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJM, Thomas DY. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57*. J Biol Chem 1998;273:6009-6012.
29. 2-microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins. Mol Immunol 1997;34:401-408.
30. 30. Suh W, Cohen-Doyle MF, Froh K, Wang K, Peterson PA, Williams DB. Interaction of MHC class I molecules with the transporter associated with antigen processing. Science 1994;264:1322-1326.
31. 31. Ortmann B, et al. A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science 1997;277:1306-1309.
32. 32. Li S, Sjogren H, Hellman U, Pettersson RF, Wang P. Cloning and functional characterization of a subunit of the transporter associated with antigen processing. Proc Natl Acad Sci USA 1997;94:8708-8713.
33. 33. Herberg JA, et al. Genomic analysis of the tapasin gene, located close to the TAP loci in the MHC. Eur J Immunol 1998;28:459-467.
34. 34. Lehner PJ, Surman MJ, Cresswell P. Soluble tapasin restores MHC class I expression and function in the tapasin negative cell line .220. Immunity 1998;8:221-231.
35. 2-microglobulin. J Biol Chem 1995;270:19638-19642.
36. 2-microglobulin, class I heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing. J Immunology 1997;158:2236-2241.
37. 37. Bangia N, Lehner PJ, Hughes EA, Surman M, Cresswell P. The N-terminal region of tapasin is required to stabilize the MHC class I loading complex. Eur J Immunol (In press).
38. 38. Elliott T, Elvin J, Cerundolo V, Allen H, Townsend A. Structural requirements for the peptide-induced conformational change of free major histocompatibility complex class I heavy chains. Eur J Immunol 1992;22:2085-2091.
39. 39. Peace-Brewer AL, Tussey LG, Matsui M, Li G, Quinn DG, Frelinger JA. A point mutation in HLA-A0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL. Immunity 1996;4:505-514.
40. 40. Lewis JW, Neisig A, Neefjes J, Elliott T. Point mutations in the α2 domain of HLA-A2.1 define a functionally relevant interaction with TAP. Curr Biol 1996;6:873-883.
41. 41. Kulig K, Nandi D, Bacik I, Monaco JJ, Vukmanovic S. Physical and functional association of the major histocompatibility complex class I heavy chain α3 domain with the transporter associated with antigen processing. J Exp Med 1998;187:865-874.
42. 42. Carreno BM, Solheim JC, Harris M, Stroynowski I, Connolly JM, Hansen TH. TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. J Immunol 1995;155:4726-4733.
43. 43. Suh WK, Mitchell EK, Yang Y, Peterson PA, Williams DB. MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains. J Exp Med 1996;184:337-348.
44. 44. Warburton RJ, et al. Mutation of the a2 domain disulfide bridge of the class I molecule HLA-A*0201 effect on maturation and peptide presentation. Hum Immunol 1994;39:261-271.
45. 45. Copeman J, Bangia N, Cross JC, Cresswell P. Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene. Eur J Immunol 1998;28:3783-3791.
46. 46. Peh CA, et al. HLA-B27-Restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptde loading. Immunity 1998;8:531-542.
47. 47. Grandea AG, Lehner PJ, Cresswell P, Spies T. Regulation of MHC class I heterodimer stability and interaction with TAP by tapasin. Immunogenetics 1997;46:477-483.
48. 48. Li S, Paulsson KM, Sjogren H-O, Wang P. Peptide-bound major histocompatibility complex class I molecules associate with tapasin before dissociation from transporter associated with antigen processing. J Biol Chem 1999;274:8649-8654.
49. 49. Roche PA, Cresswell P. Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding. Nature 1990;345:615-618.
50. 50. Newcomb JR, Cresswell P. Characterization of endogenous peptides bound to purified HLA-DR molecules and their absence from invariant chain-associated αβ dimers. J Immunol 1993;150:499-507.
51. 51. Denzin LK, Hammond C, Cresswell P. HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules. J Exp Med 1996;184:2153-2165.
52. 52. Kropshofer H, Arndt SO, Moldenhauer G, Hammerling GJ, Vogt AB. HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH. Immunity 1997;6:293-306.