Thymoproteasome: probable role in generating positively selecting peptides

Current Opinion in Immunology

Volumn 20, Issue 2, 2008, Pages 192-196

  Murata, Shigeo ^a   Takahama, Yousuke ^b   Tanaka, Keiji ^c  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF TOKUSHIMA   (Japan)

^c TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDASE; PEPTIDE DERIVATIVE; PROTEASOME; THYMOPROTEASOME;

ANTIGEN PRESENTATION; CD8+ T LYMPHOCYTE; CELL MATURATION; CELL SELECTION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; EPITHELIUM CELL; EUKARYOTE; NONHUMAN; PROTEIN EXPRESSION; PROTEIN FUNCTION; REVIEW; THYMOCYTE; THYMUS; VERTEBRATE;

ANIMALS; ANTIGEN PRESENTATION; CD8-POSITIVE T-LYMPHOCYTES; EPITHELIAL CELLS; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; MICE; PEPTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; THYMUS GLAND;

EID: 44749085669     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coi.2008.03.002     Document Type: Review

References (23)

1. Coux O., Tanaka K., and Goldberg A.L. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 65 (1996) 801-847
2. Kloetzel P.M. The proteasome and MHC class I antigen processing. Biochim Biophys Acta 1695 (2004) 225-233
3. Tanaka K., and Kasahara M. The MHC class I ligand-generating system: roles of immunoproteasomes and the interferon-gamma-inducible proteasome activator PA28. Immunol Rev 163 (1998) 161-176
4. Murata S., Sasaki K., Kishimoto T., Niwa S., Hayashi H., Takahama Y., and Tanaka K. Regulation of CD8+ T cell development by thymus-specific proteasomes. Science 316 (2007) 1349-1353. This paper reports the discovery of a novel proteasome subunit named β5t exclusively expressed in cTECs that plays a crucial role in the development of CD8 T cells in the thymus. This work strongly suggests that cTECs are equipped with specialized capacity to present unique peptide repertoire for positive selection of thymocytes.
5. Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82 (2002) 373-428
6. Van Kaer L., Ashton-Rickardt P.G., Eichelberger M., Gaczynska M., Nagashima K., Rock K.L., Goldberg A.L., Doherty P.C., and Tonegawa S. Altered peptidase and viral-specific T cell response in LMP2 mutant mice. Immunity 1 (1994) 533-541
7. Fehling H.J., Swat W., Laplace C., Kuhn R., Rajewsky K., Muller U., and von Boehmer H. MHC class I expression in mice lacking the proteasome subunit LMP-7. Science 265 (1994) 1234-1237
8. Basler M., Moebius J., Elenich L., Groettrup M., and Monaco J.J. An altered T cell repertoire in MECL-1-deficient mice. J Immunol 176 (2006) 6665-6672
9. Baumeister W., Walz J., Zuhl F., and Seemuller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92 (1998) 367-380
10. Beninga J., Rock K.L., and Goldberg A.L. Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J Biol Chem 273 (1998) 18734-18742
11. Rock K.L., York I.A., and Goldberg A.L. Post-proteasomal antigen processing for major histocompatibility complex class I presentation. Nat Immunol 5 (2004) 670-677
12. Groll M., Ditzel L., Lowe J., Stock D., Bochtler M., Bartunik H.D., and Huber R. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386 (1997) 463-471
13. Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., and Tsukihara T. The structure of the mammalian 20S proteasome at 2.75 A resolution. Structure 10 (2002) 609-618. This paper demonstrates for the first time the structure of the mammalian 20S proteasome. The possible mechanism of specialized catalytic activity of the immunoproteasome is discussed.
14. Nil A., Firat E., Sobek V., Eichmann K., and Niedermann G. Expression of housekeeping and immunoproteasome subunit genes is differentially regulated in positively and negatively selecting thymic stroma subsets. Eur J Immunol 34 (2004) 2681-2689
15. Starr T.K., Jameson S.C., and Hogquist K.A. Positive and negative selection of T cells. Annu Rev Immunol 21 (2003) 139-176
16. Hogquist K.A., Baldwin T.A., and Jameson S.C. Central tolerance: learning self-control in the thymus. Nat Rev Immunol 5 (2005) 772-782
17. Gallegos A.M., and Bevan M.J. Central tolerance: good but imperfect. Immunol Rev 209 (2006) 290-296
18. Anderson M.S., Venanzi E.S., Klein L., Chen Z., Berzins S.P., Turley S.J., von Boehmer H., Bronson R., Dierich A., Benoist C., et al. Projection of an immunological self shadow within the thymus by the AIRE protein. Science 298 (2002) 1395-1401
19. Ashton-Rickardt P.G., Bandeira A., Delaney J.R., Van Kaer L., Pircher H.P., Zinkernagel R.M., and Tonegawa S. Evidence for a differential avidity model of T cell selection in the thymus. Cell 76 (1994) 651-663
20. Hogquist K.A., Jameson S.C., Heath W.R., Howard J.L., Bevan M.J., and Carbone F.R. T cell receptor antagonist peptides induce positive selection. Cell 76 (1994) 17-27
21. Honey K., Nakagawa T., Peters C., and Rudensky A. Cathepsin L regulates CD4+ T cell selection independently of its effect on invariant chain: a role in the generation of positively selecting peptide ligands. J Exp Med 195 (2002) 1349-1358. This paper suggests that cathepsin L is required for production of positively selecting peptides for MHC class II-restricted T cells in cTECs.
22. Hogquist K.A., Tomlinson A.J., Kieper W.C., McGargill M.A., Hart M.C., Naylor S., and Jameson S.C. Identification of a naturally occurring ligand for thymic positive selection. Immunity 6 (1997) 389-399
23. Hu Q., Bazemore Walker C.R., Girao C., Opferman J.T., Sun J., Shabanowitz J., Hunt D.F., and Ashton-Rickardt P.G. Specific recognition of thymic self-peptides induces the positive selection of cytotoxic T lymphocytes. Immunity 7 (1997) 221-231