A proteolytic system that compensates for loss of proteasome function

Nature

Volumn 392, Issue 6676, 1998, Pages 618-622

  Glas, Rickard ^a,b   Bogyo, Matthew ^a,b   McMaster, John S ^a,c   Gaczynska, Maria ^a,d   Ploegh, Hidde L ^a,b  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; PROTEINASE;

ANIMAL CELL; ARTICLE; CELL CYCLE; ENZYME ACTIVITY; ENZYME SUBUNIT; GROWTH REGULATION; LYMPHOMA CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING;

ADAPTATION, PHYSIOLOGICAL; ANIMALS; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; ENDOPEPTIDASES; HISTOCOMPATIBILITY ANTIGENS CLASS I; HYDROLYSIS; MICE; MULTIENZYME COMPLEXES; PROTEASOME ENDOPEPTIDASE COMPLEX; SULFONES; THERMOPLASMA; TUMOR CELLS, CULTURED; UBIQUITINS;

ANIMALIA; MAMMALIA;

EID: 0032499199     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/33443     Document Type: Article

References (29)

1. Etlinger, J. D. & Goldberg, A. L. A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes. Proc. Natl Acad. Sci. USA 74, 54-58 (1977).
2. Palombella, V. J., Rando, O. J., Goldberg, A. L. & Maniatis, T. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78, 773-785 (1994).
3. Glotzer, M., Murray, A. W. & Kirschner, M. W. Cyclin is degraded by the ubiquitin pathway. Nature 349, 132-138 (1991).
4. Rock, K. L. et al. Inhibition of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-771 (1994).
5. Coux, O., Tanaka, K. & Goldberg, A. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847 (1996).
6. Seemuller, E. et al. The proteasome from Thermoplasma acidophilum: A threonine protease. Science 268, 579-582 (1995).
7. Löwe, J. et al. Crystal structure of the 20S proteasome from the Archaeon T. acidophilum at 3.4Å resolution. Science 268, 533-539 (1995).
8. Omura, S. et al. Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells. J. Antibiot. 44, 113-116 (1991).
9. Fenteany, G. et al. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-730 (1995).
10. Dick, L. R. et al. Mechanistic studies on the inactivation of the proteasome by lactacystin. J. Biol. Chem. 271, 7273-7276 (1996).
11. Groll, M. et al. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386, 463-471 (1997).
12. Bogyo, M. et al. Covalent modification of the active site Thr of proteasomeal β-subunits and the E. coli homolog HslV by a new class of inhibitors. Proc. Natl Acad. Sci., USA 94, 6629-6634 (1997).
13. Nandi, D., Woodward, E., Ginsburg, D. B. & Monaco, J. J. Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor beta subunits. EMBO J. 16, 5363-5375 (1997).
14. Driscoll, J., Brown, M. G., Finley, D. & Monaco, J. J. MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 365, 262-264 (1993).
15. Gaczynska, M., Rock, K. L. & Goldberg, A. γ-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 365, 264-267 (1993).
16. Craiu, A.C. et al. Lactacystin and clasto-lactacystin β-lactone modify multiple proteasome β subunits and inhibit intracellular protein degradation and MHC class I antigen presentation. J. Biol. Chem. 272, 13437-13445 (1997).
17. Bai, A. & Forman, J. The effect of proteasome inhibitor lactacystin on the presentation of transporter associated with antigen processing (TAP)-dependent and TAP-independent peptide epitopes by class I molecules. J. Immunol. 159, 2139-2146 )1007).
18. Vinitsky, A. et al. The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors: involvement of non-proteasomal cytosolic proteases in antigen processing? J. Immunol. 159, 554-564 (1997).
19. Hilt, W. & Wolf, D. H. Proteasomes of the yeast S. cerevisiae: genes, structure and function. Mol. Biol. Rep. 21, 3-10 (1995).
20. Ghislain, M., Udvardy, A. & Mann, C. et al. S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature 366, 358-362 (1993).
21. Gordon, C., McGurk, G., Dilion, P., Rosen, C. & Hastie, N. D. Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit. Nature 366, 355-357 (1993).
22. Tamura, T. et al. Tricorn protease - the core of a modular proteolytic system. Science 274, 1385-1389 (1996).
23. Kettner, C. & Shaw, E. Inactivation of trypsin-like enzymes with peptides of arginine chloromethyl ketone. Meth. Enzymol. 80, 826-842 (1981).
24. Drexler, H. C. A. Activation of the cell death program by inhibition of proteasome function. Proc. Natl Acad. Sci. USA 94, 855-860 (1997).
25. Hershko, A. & Ciechanover, A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61, 761-807 (1992).
26. King, R. W., Jackson, P. K. & Kirschner, M. W. Mitosis in transition. Cell 79, 563-571 (1994).
27. Sheaff, R. & Roberts, J. M. End of the line: proteolytic degradation of cyclin-dependent kinase inhibitors. Chem. Biol. 3, 869-873 (1996).
28. b determined with monoclonal antibodies and H-2 mutant mice. Proc. Natl Acad. Sci. USA 79, 4737-4741 (1982).
29. Ljunggren, H.-G. et al. Empty MHC class 1 molecules come out in the cold. Nature 346, 476-480 (1990).