Mechanisms and regulation of ubiquitin-mediated cyclin degradation

Advances in Experimental Medicine and Biology

Volumn 389, Issue , 1996, Pages 221-227

  Hershko, Avram ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; UBIQUITIN;

ANIMAL; CELL CYCLE; HYDROLYSIS; METABOLISM; PHYSIOLOGY; REVIEW; AMINO ACID SEQUENCE; CARBOXY TERMINAL SEQUENCE; CONFERENCE PAPER; HYDROPHOBICITY; LIGATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; YEAST;

ANIMALS; CELL CYCLE; CYCLINS; HYDROLYSIS; UBIQUITINS;

EID: 0030337875     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4613-0335-0_27     Document Type: Article

References (40)

1. Hershko, A., and Ciechanover, A. (1992). The Ubiquitin System for Protein Degradation. Annu. Rev. Biochem. 61, 761-807.
2. Finley, D. and Chau, V. (1991). Ubiquitination. Annu. Rev. Cell Biol. 7, 25-69.
3. Rechsteiner, M. (1993). The Multicatalytic and 26S Proteases. J. Biol. Chem. 268, 6065-6068.
4. Pickart, C.M. and Rose, I.A. (1985). Functional Heterogeneity of Ubiquitin Carrier Proteins. J. Biol. Chem. 260, 1573-1581.
5. Jentsch, S. (1992). The Ubiquitin-Conjugation System. Annu. Rev. Genet. 26, 179-207.
6. Hershko, A., Heller, H. Eytan, E. and Reiss, Y. (1986). The Protein Substrate Binding Site of the Ubiquitin-Protein Ligase System. J. Biol. Chem. 261, 11992-11999.
7. Reiss, Y., Heller, H. and Hershko, A., (1989). Binding Sites of Ubiquitin-Protein Conjugates and of Ubiquitin-Carrier Protein. J. Biol. Chem. 264, 10378-10383.
8. 2-terminal Residue of Proteins to Ubiquitin-Protein Ligase: Use of Amino Acid Derivatives to Characterize Specific Binding Sites. J. Biol. Chem. 263, 2693-2698.
9. 2-Terminal Binding Sites on a Single Enzyme. J. Biol. Chem. 265, 3685-3690.
10. Heller, H. and Hershko, A., (1990). A Ubiquitin-Protein Ligase Specific for Type III Protein Substrates. J. Biol. Chem. 265, 6532-6535.
11. Hershko, A., and Heller, H. (1985). Occurrence of a Polyubiquitin Structure in Ubiquitin-Protein Conjugates. Biochem. Biophys. Res. Commun. 128, 1079-1086.
12. Chau, V., Tobias, J. W., Bachmair, A., Mariott, D., Ecker, D., Gonda, D.K. and Varshavsky, A. (1989). A Multiubiquitin Chain is Confined to a Specific Lysine in a Targeted Short-lived Protein. Science, 243, 1576-1583.
13. Hough, R., Pratt, G. and Rechsteiner, M. (1987). Purification of Two High Molecular Weight Proteases from Rabbit Reticulocyte Lysate. J. Biol. Chem. 262, 8308-8313.
14. Ganoth, D., Leshinsky, E., Eytan, E. and Hershko, A. (1988). A Multicomponent System that Degrades Proteins Conjugated to Ubiquitin: Resolution of Factors and Evidence for ATP-Dependent Complex Formation. J. Biol. Chem. 263, 12412-12419.
15. Eytan, E., Ganoth, D., Armon, T. and Hershko, A., (1989). ATP-Dependent Incorporation of 20S Protease Into the 26S Complex that Degrades Proteins Conjugated to Ubiquitin. Proc. Natl. Acad Sci. USA. 86, 7751-7755.
16. Deleted.
17. Armon, T., Ganoth, D. and Hershko, A., (1990). Assembly of the 26S Complex That Degrades Proteins Ligated to Ubiquitin is Accompanied by the Formation of ATPase Activity. J. Biol. Chem. 265, 20723-20726.
18. Shanklin, J., Jabben, M., and Vierstra, R.D. (1987). Red Light-Induced Formation of Ubiquitin-Phytochrome Conjugates: Identification of Possible Intermediates of Phytochrome Degradation. Proc. Natl. Acad Sci. USA 84, 359-363.
19. Hochstrasser, M., Ellison, M.J., Chau, V. and Varshavsky, A. (1991). The Short-lived MATα2 Transcriptional Regulator is Ubiquitinated In Vivo. Proc. Natl. Acad Sci. USA, 88, 4606-4610.
20. Palombella, V.J., Rando, O.J., Goldberg, A. L. and Maniatis, T. (1994). The Ubiquitin-Proteasome Pathway is Required for the Processing of NF-κB Precursor Protein and the Activation of NF-κB. Cell. 78, 773-785.
21. Michalek, M., Grant, E., Gramm, C., Goldberg, A.L. and Rock, K. (1993). A Role for Ubiquitin-dependent Proteolytic Pathway in MHC class-I-restricted Antigen Presentation. Nature. 363, 552-554.
22. Scheffner, M., Huigbretze, J.M., Vierstra, R.D. and Howley, P. (1993). The HPV-16 E6 and E6-AP Complex Functions as a Ubiquitin-Protein Ligase in the Ubiquitination of p53. Cell, 75, 495-505.
23. Ciechanover, A., Di Giuseppe, J.A., Bercovitch, B., Orian, A., Richter, J.D., Schwartz, A.L. and Brodner, G.M. (1991). Degradation of Oncoproteins by the Ubiquitin System In Vitro. Proc. Natl. Acad Sci. USA 88, 139-143.
24. Treier, M., Staszerwski, L.M. and Bohmann, D. (1994) Ubiquitin-Dependent c-jun Degradation In Vivo is Mediated by the δ Domain. Cell. 78, 787-798.
25. 2 in Mos. EMBO J. 12, 4021-4027.
26. Glotzer, M., Murray, A.W. and Kirschner M.W. (1991). Cyclin is Degraded by the Ubiquitin Pathway. Nature, 349, 132-138.
27. Hershko, A., Ganoth, D., Pehrson, J., Palazzo, R.E. and Cohen, L.H. (1991). Methylated Ubiquitin Inhibits Cyclin Degradation in Clam Embryo Extracts. J. Biol. Chem. 266 16376-116379.
28. sicl Controls the G1 to S Transition in S cerevisiae. Cell. 79, 233-244.
29. Bachmair, A., Finley, D., and Varshavsky, A. (1986). In Vivo Half-Life of a Protein is a Function of its Amino-terminal Residue. Science. 234, 179-186.
30. Barbel, B., Wunning, I. and Varshavsky, A. (1990). The Recognition Component of the N-End Rule Pathway. EMBO J. 9, 3179-3189.
31. Norbury C. and Nurse, P. (1992). Animal Cell Cycles and their Control. Annu. Rev. Biochem. 61, 441-470.
32. King, W.R., Jackson, P.K. and Kirschner, M.W. (1994). Mitosis in Transition. Cell, 79, 563-571.
33. Murry, A.W., Solomon, M.J. and Kirschner, M.W. (1989). The Role of Cyclin Synthesis and Degradation in the Control of Maturation Promoting Activity. Nature, 339, 280-286.
34. Luca, F.C. and Ruderman, J.V. (1989). Control of Programmed Cyclin Destruction in a Cell-Free System. J. Biol. Chem. 109, 1895-1909.
35. Luca, F.C., Shibuya, E.K., Dohrmann, C.D. and Ruderman, J.V. (1991). Both Cyclin AΔ60 and BΔ97 are Stable and Arrest Cells at the M-phase, but only Cyclin BΔ97 Turns on Cyclin Destruction. EMBO J. 10, 4311-4320.
36. Felix, M.A., Labbe, J.C., Doree, M., Hunt, T. and Karsenti, E. (1990). Triggering of Cyclin Degradation in Interphase Extracts of Amphibian Eggs by Cdc2 Kinase. Nature, 346, 379-382.
37. Hershko, A., Ganoth, D., Sudakin, V., Cohen, L.H., Luca, F.C., Ruderman, J.V. and Eytan, E. (1994). Components of a System that Ligates Cyclin to Ubiquitin and Their Regulation by Protein Kinase Cdc2. J. Biol. Chem. 269, 4940-4946.
38. Sudakin, V., Ganoth, D., Dahan, A., Heller, H., Hershko, J., Luca, F.C., Ruderman, J.V. and Hershko, A. (1995). The Cyclosome, a Large Complex Containing Cyclin-Selective Ubiquitin Ligase Activity, Targets Cyclins for Destruction at the End of Mitosis. Mol. Biol. Cell, in press.
39. Lorca, T., Fesquet, D., Zindy, F., LeBouffant, F., Cerutti, M., Brechot, C., Devauchelle, G. and Doree, M. (1991). An Okadaic Acid-sensitive Phosphatase Negatively Controls the Cyclin Degradation Pathway in Amphibian Eggs. Mol. Cell Biol. 11, 1171-1175.
40. Cohen, P., Holmes, C.F.B. and Tsukitani, Y. (1990). Okadaic acid: a New Probe for the Study of Cellular Regulation. Trends Biochem. Sci. 15, 98-102.