Deubiquitinating Enzyme Ubp6 Functions Noncatalytically to Delay Proteasomal Degradation

Cell

Volumn 127, Issue 1, 2006, Pages 99-111

  Hanna, John ^a   Hathaway, Nathaniel A ^a   Tone, Yoshiko ^a   Crosas, Bernat ^a,b   Elsasser, Suzanne ^a   Kirkpatrick, Donald S ^a   Leggett, David S ^a   Gygi, Steven P ^a   King, Randall W ^a   Finley, Daniel ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b INSTITUT DE BIOLOGIA MOLECULAR DE BARCELONA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; CANAVANINE; CYCLIN B; EPOXOMICIN; POLYPEPTIDE; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN; PROTEIN RPN 11; PROTEIN SUBUNIT; PROTEIN UBP 6; RAPAMYCIN; UBIQUITIN; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; DRUG EFFECT; ENZYME INHIBITION; GENE OVEREXPRESSION; HUMAN; NERVOUS SYSTEM INJURY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; UBIQUITINATION; YEAST;

EID: 33749049581     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2006.07.038     Document Type: Article

References (28)

1. Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 5 (2004) 417-421
2. Borodovsky A., Kessler B.M., Casagrande R., Overkleeft H.S., Wilkinson K.D., and Ploegh H.L. A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO J. 20 (2001) 5187-5196
3. Chernova T.A., Allen K.D., Wesoloski L.M., Shanks J.R., Chernoff Y.O., and Wilkinson K.D. Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. J. Biol. Chem. 278 (2003) 52102-52115
4. Cochella L., and Green R. Fidelity in protein synthesis. Curr. Biol. 15 (2005) R536-R540
5. Elsasser S., Chandler-Militello D., Muller B., Hanna J., and Finley D. Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J. Biol. Chem. 279 (2004) 26817-26822
6. Elsasser S., and Finley D. Delivery of ubiquitinated substrates to protein-unfolding machines. Nat. Cell Biol. 7 (2005) 742-749
7. Glickman M.H., Rubin D.M., Coux O., Wefes I., Pfeifer G., Cjeka Z., Baumeister W., Fried V.A., and Finley D. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94 (1998) 615-623
8. Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 426 (2003) 895-899
9. 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
10. Guterman A., and Glickman M.H. Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J. Biol. Chem. 279 (2004) 1729-1738
11. Hanna J., Leggett D.S., and Finley D. Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Mol. Cell. Biol. 23 (2003) 9251-9261
12. Hu M., Li P., Song L., Jeffrey P.D., Chernova T.A., Wilkinson K.D., Cohen R.E., and Shi Y. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. EMBO J. 24 (2005) 3747-3756
13. Johnson E.S., Ma P.C., Ota I.M., and Varshavsky A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270 (1995) 17442-17456
14. Joyce C.M., and Benkovic S.J. DNA polymerase fidelity: kinetics, structure, and checkpoints. Biochemistry 43 (2004) 14317-14324
15. Kirkpatrick D.S., Hathaway N.A., Hanna J., Elsasser S., Rush J., Finley D., King R.W., and Gygi S.P. Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology. Nat. Cell Biol. 8 (2006) 700-710
16. Kisselev A.F., Callard A., and Goldberg A.L. Importance of the proteasome's different proteolytic sites and the efficacy of inhibitors varies with the protein substrate. J. Biol. Chem. 281 (2006) 8582-8590
17. Lam Y.A., Xu W., DeMartino G.N., and Cohen R.E. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385 (1997) 737-740
18. Leggett D.S., Hanna J., Borodovsky A., Crosas B., Schmidt M., Baker R.T., Walz T., Loegh H., and Finley D. Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10 (2002) 495-507
19. Maytal-Kivity V., Reis N., Hofmann K., and Glickman M.H. MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC Biochem. 3 (2002) 28
20. Miura T., and Abe F. Multiple ubiquitin-specific protease genes are involved in degradation of yeast tryptophan permease Tat2 at high pressure. FEMS Microbiol. Lett. 239 (2004) 171-179
21. Pickart C.M., and Cohen R.E. Proteasomes and their kin: proteases in the machine age. Nat. Rev. Mol. Cell Biol. 5 (2004) 177-187
22. Stone M., Hartmann-Petersen R., Seeger M., Bech-Otschir D., Wallace M., and Gordon C. Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast. J. Mol. Biol. 344 (2004) 697-706
23. Varshavsky A. Regulated protein degradation. Trends Biochem. Sci. 30 (2005) 283-286
24. Verma R., Chen S., Feldman R., Schieltz D., Yates J., Dohmen J., and Deshaies R.J. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 11 (2000) 3425-3439
25. Verma R., Aravind L., Oania R., McDonald W.H., Yates III J.R., Koonin E.V., and Deshaies R.J. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298 (2002) 611-615
26. Wilson S.M., Bhattacharyya B., Rachel R.A., Coppola V., Tessarollo L., Householder D.B., Fletcher C.F., Miller R.J., Copeland N.G., and Jenkins N.A. Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease. Nat. Genet. 32 (2002) 420-425
27. Wullschleger S., Loewith R., and Hall M.N. TOR signaling in growth and metabolism. Cell 124 (2006) 471-484
28. Yao T., and Cohen R.E. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419 (2002) 403-407