A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 α-subunit of the 20S proteasome

EMBO Journal

Volumn 20, Issue 10, 2001, Pages 2367-2375

  Touitou, Robert ^a   Richardson, Jo ^a   Bose, Suchira ^b   Nakanishi, Makoto ^c   Rivett, Jennifer ^b   Allday, Martin J ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF BRISTOL   (United Kingdom)

^c NAGOYA CITY UNIV MEDICAL SCHOOL   (Japan)

Author keywords

C8; Degradation signal; p21WAF1 CIP1; Proteasome

Indexed keywords

PROTEASOME; PROTEIN P21; PROTEINASE;

ALPHA CHAIN; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HALF LIFE TIME; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TARGETING; REGULATORY MECHANISM;

3T3 CELLS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL NUCLEUS; CYCLIN-DEPENDENT KINASE INHIBITOR P21; CYCLINS; CYSTEINE ENDOPEPTIDASES; HUMANS; MICE; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; PROLIFERATING CELL NUCLEAR ANTIGEN; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN FOLDING; TUMOR CELLS, CULTURED;

EID: 0035872863     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.10.2367     Document Type: Article

References (29)

1. Adams, P.D., Sellers, W.R., Sharma, S.K., Wu, A.D., Nalin, C.M. and Kaelin, W. (1996) Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors. Mol. Cell Biol., 16, 6623-6633.
2. Akioka, H., Forseberg, N.E., Ishida, N., Okumura, K., Nogami, M., Taguchi, H., Noda, C. and Tanaka, K. (1995) Isolation and characterization of the HC8 subunit gene of the human proteasome. Biochem. Biophys. Res. Commun., 207, 318-323.
3. Bain, M., Watson, R.J., Farrell, P.J. and Allday, M.J. (1996) Epstein-Barr virus nuclear antigen 3C is a powerful repressor of transcription when tethered to DNA. J. Virol., 70, 2481-2489.
4. Baumeister, W., Walz, J., Zuhl, F. and Seemuller, E. (1998) The proteasome: paradigm of a self-compartmentalizing protease. Cell, 92, 367-380.
5. WAF1/CIP1 expression. Biochem. Biophys. Res. Commun., 227, 564-569.
6. WAF1 complexes during the cell cycle. Proc. Natl Acad. Sci. USA, 95, 12254-12259.
7. Cayrol, C. and Ducommun, B. (1998) Interaction with cyclin-dependent kinases and PCNA modulates proteasome-dependent degradation of p21. Oncogene, 17, 2437-2444.
8. Gerards, W.L.H., de Jong, W.W., Bloemendal, H. and Boelens, W. (1998) The human proteasomal subunit HsC8 induces ring formation of other A-type subunits. J. Mol. Biol., 275, 113-121.
9. Groll, M., Ditzel, L., Lowe, J., Stock, D., Bochtler, M., Bartunick, H.D. and Huber, R. (1997) Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature, 386, 463-471.
10. Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc. Natl Acad. Sci. USA, 93, 11504-11509.
11. Waf1/Cip1/Sdi1. J. Chromatogr. A, 777, 23-30.
12. Kroll, M. et al. (1997) The carboxy-terminus of IκBα determines susceptibility to degradation by the catalytic core of the proteasome. Oncogene, 15, 1841-1850.
13. Maki, C.G. and Howley, P.M. (1997) Ubiquitination of p53 and p21 is differentially affected by ionizing and UV radiation. Mol. Cell. Biol., 17, 355-363.
14. Masson, P., Andersson, O., Petersen, U.-M. and Young, P. (2001) Identification and characterisation of a Drosophila nuclear proteasome regulator. J. Biol. Chem., 276, 1383-1390.
15. Murata, S., Kawahara, H., Tohma, S., Yamamoto, K., Kasahara, M., Nabeshima, Y., Tanaka, K. and Chibas, T., (1999) Growth retardation in mice lacking the proteasome activator PA28γ. J. Biol. Chem., 274, 38211-38215.
16. SDI1/WAF1/CIP1 is involved in proliferating cell nuclear antigen binding but does not appear to be required for growth inhibition. J. Biol. Chem., 270, 17060-17063.
17. Radkov, S.A., Bain, M., Farrell, P.J., West, M., Rowe, M. and Allday, M.J. (1997) Epstein-Barr virus EBNA 3C represses Cp, the major promoter for EBNA expression, but has no effect on the promoter of the cell gene CD21. J. Virol., 71, 8552-8562.
18. Radkov, S.A., Touitou, R., Brehm, A., Rowe, M., West, M., Kouzarides, T. and Allday, M.J. (1999) Epstein-Barr virus nuclear antigen 3C interacts with histone deacetylase to repress transcription. J. Virol., 73, 5688-5697.
19. Rivett, A.J., Savory, P.J. and Djahallah, N. (1994) Multicatalytic endopeptidase complex (proteasome). Methods Enzymol., 244, 331-350.
20. Rousseau, D., Cannnella, D., Boulaire, J., Fitzgerald, P., Fotedar. A. and Fotedar, R. (1999) Growth inhibition by CDK-cyclin and PCNA binding domains of p21 occurs by distinct mechanisms and is regulated by ubiquitin-proteasome pathway. Oncogene, 18, 4313-4325.
21. Rousset, R., Desbois, C., Bantignies, F. and Jalinot, P. (1996) Effects on NFκB1/p105 processing of the interaction between the HTLV1 transactivator Tax and the proteasome. Nature, 381, 328-331.
22. Cip1 ubiquitination. Mol. Cell, 5, 403-410.
23. Sherr, C.J. and Roberts, J.M. (1995) Inhibitors of mammalian G1 cyclin-dependent kinases. Genes Dev., 9, 1149-1163.
24. Sherr, C.J. and Roberts, J.M. (1999) CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev., 13, 1501-1512.
25. Tamura, T., Lee, D.H., Osaka, F., Fujiwara, T., Shin, S., Chung, C.H., Tanaka, K. and Ichihara, A. (1991) Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes). Biochem. Biophys. Acta, 1089, 95-102.
26. Thrower, J.S., Hoffman, L., Rechsteiner, M. and Pickart, C.M. (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J., 19, 94-102.
27. Verma, R. and Deshaies, R.J. (2000) A proteasome howdunit: the case of the missing signal. Cell, 101, 341-344.
28. Wade, M. and Allday, M.J. (2000) Epstem-Barr virus suppresses a G2/M checkpoint activated by genotoxins. Mol. Cell. Biol., 20, 1344-1360.
29. Wickner, S., Maurizi, M.R. and Gottesman, S. (1999) Post-translational quality control: folding, refolding and degrading proteins. Science, 286, 1888-1893.