A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly

Cell

Volumn 96, Issue 5, 1999, Pages 635-644

  Koegl, Manfred ^a   Hoppe, Thorsten ^b   Schlenker, Stephan ^c   Ulrich, Helle D ^b   Mayer, Thomas U ^d   Jentsch, Stefan ^b  

^a Axaron Bioscience AG   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c GPC AG   (Germany)

^d HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LIGASE; PROTEASOME; REGULATOR PROTEIN; UBIQUITIN;

ANIMAL CELL; ARTICLE; CATALYSIS; CELL FUNCTION; CELL SURVIVAL; CONTROLLED STUDY; ENZYME SPECIFICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN FAMILY; REGULATORY MECHANISM; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

ANIMALIA; DICTYOSTELIUM; EUKARYOTA;

EID: 0033525589     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80574-7     Document Type: Article

References (27)

1. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidmna, J.G., Smith, J.A., and Struhl, K. (1994). Current Protocols in Molecular Biology (New York: Green and Wiley).
2. Biggins, S., Ivanovska, I., and Rose, M.D. (1996). Yeast ubiquitinlike genes are involved in duplication of the microtubule organizing center. J. Cell Biol. 133, 1331-1346.
3. Chau, V., Tobias, J.W., Bachmair, A., Marriott, D., Ecker, D.J., Gonda, D.K., and Varshavsky, A. (1989). A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576-1583.
4. Cook, W.J., Jeffrey, L.C., Kasperek, E., and Pickart, C.M. (1994). Structure of tetraubiquitin shows how multiubiquitin chains can be formed. J. Mol. Biol. 236, 601-609.
5. Dai, R.-M., Chen, E., Longo, D.L., Gorbea, C.M., and Li, C.-C.H. (1998). Involvement of valosin-containing protein, an ATPase copurified with IκBα and the 26S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα. J. Biol. Chem. 273, 3562-3573.
6. Finley, D., Özkaynak, E., and Varshavsky, A. (1985). The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell 48, 1035-1046.
7. Fröhlich, K.-U., Fries, H.W., Rüdiger, M., Erdmann, R., Botstein, D., and Mecke, D. (1991). Yeast cell cycle protein Cdc48p shows full length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression. J. Cell Biol. 114, 443-453.
8. Ghislain, M., Dohmen, R.J., Levy, F., and Varshavsky, A. (1996). Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EM BO J. 15, 4884-4899.
9. Hochstrasser, M. (1996). Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439.
10. Jentsch, S., and Schlenker, S. (1995). Selective protein degradation: a journey's end within the proteasome. Cell 82, 881-884.
11. Jentsch, S., McGrath, J.P., and Varshavsky, A. (1987). The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329, 131-134.
12. Johnson, E.S., Bartel, B., Seufert, W., and Varshavsky, A. (1992). Ubiquitin as a degradation signal. EMBO J. 11, 497-505.
13. Johnson, E.S., Ma, P.C.M., Ota, I., and Varshavsky, A. (1995). A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456.
14. Jungmann, J., Reins, H.-A., Schobert, C., and Jentsch, S. (1993). Resistance to cadmium mediated by ubiquitin-dependent proteolysis. Nature 367, 369-371.
15. Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., and Shimizu, N. (1998). Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392, 605-608.
16. Masutani, C., Sugasawa, K., Yanagisawa, J., Sonoyama, T., Ui, M., Enomoto, T., Takio, K., Tanaka, K., van der Spek, P.J., and Bootsma, D., et al. (1994). Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. EM BO J. 13, 1831-1843.
17. McGrath, J.P., Jentsch, S., and Varshavsky, A. (1991). UBA1: an essential yeast gene encoding ubiquitin-activating enzyme. EM BO J. 10, 227-236.
18. Mortz, E., Vorm, O., Mann, M., and Roepstorff, P. (1994). Identification of proteins in polyacrylamide gels by mass spectrometric peptide mapping combined with database search. Biol. Mass. Spectrom. 23, 249-261.
19. Patton, E.E., Willems, A.R., and Tyers, M. (1998). Combinatorial control in ubiquitin-dependent proteolysis: don't Skp the F-box hypothesis. Trends Genet. 14, 236-242.
20. Pukatzki, S., Tordilla, N., Franke, J., and Kessin, R.H. (1998). A novel component involved in ubiquitination is required for development of Dictyostelium discoideum. J. Biol. Chem. 273, 24131-24138.
21. Schauber, C., Chen, L., Tongaonkar, P., Vega, I., Lambertson, D., Potts, W., and Madura, K. (1998). Rad23 links DNA repair to the ubiquitin proteasome pathway. Nature 391, 715-718.
22. Scheffner, M., Nuber, U., and Huibregtse, J.M. (1995). Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 373, 81-83.
23. Seufert, W., and Jentsch, S. (1990). Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EM BO J. 9, 543-550.
24. Seufert, W., and Jentsch, S. (1992). In vivo function of the proteasome in the ubiquitin pathway. EM BO J. 11, 3077-3080.
25. Sung, P., Prakash, S., and Prakash, L. (1988). The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histories, and its acidic domain mediates this activity. Genes Dev. 2, 1476-1485.
26. van Nocker, S., Sadis, S., Rubin, D.M., Glickman, M., Fu, H., Coux, O., Wefes, I., Finley, D., and Viestra, R.D. (1996). The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16, 6020-6028.
27. Watkins, J.F., Sung, P., Prakash, L., and Prakash, S. (1993). The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function. Mol. Cell. Biol. 13, 7757-7765.