Deubiquitinating enzymes: Their roles in development, differentiation, and disease

International Review of Cytology

Volumn 229, Issue , 2003, Pages 43-72

  Fischer, Janice A ^a  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

Deubiquitinating enzyme; Dub; Proteolysis; Ubiquitin; Ubp; Uch

Indexed keywords

PHOSPHATASE; UBIQUITIN PROTEIN LIGASE; BETA CATENIN; CANOE PROTEIN, DROSOPHILA; CTNNB1 PROTEIN, HUMAN; CYTOSKELETON PROTEIN; DROSOPHILA PROTEIN; FUNGAL PROTEIN; KINESIN; MLLT4 PROTEIN, HUMAN; MYOSIN; PROTEINASE; PROTOZOAL PROTEIN; TRANSACTIVATOR PROTEIN; UBIQUITIN;

CELL FUNCTION; CHEMICAL BOND; DEVELOPMENT; DISEASE COURSE; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN DEFECT; PROTEIN DEGRADATION; REGULATORY MECHANISM; REVIEW; UBIQUITINATION; ANIMAL; DEGENERATIVE DISEASE; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; HUMAN; METABOLISM; NEOPLASM; PHOTORECEPTOR; PHYSIOLOGY; ULTRASTRUCTURE;

ANIMALS; BETA CATENIN; CELL PHYSIOLOGY; CYTOSKELETAL PROTEINS; DROSOPHILA PROTEINS; ENDOPEPTIDASES; FUNGAL PROTEINS; HUMANS; KINESIN; MYOSINS; NEOPLASMS; NEURODEGENERATIVE DISEASES; PHOTORECEPTORS, INVERTEBRATE; PROTOZOAN PROTEINS; SUBSTRATE SPECIFICITY; TRANS-ACTIVATORS; UBIQUITIN;

EID: 1542786907     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(03)29002-1     Document Type: Article

References (103)

1. Amerik, A. Y., Swaminathan, S., Krantz, B. A., Wilkinson, K. D., and Hochstrasser, M. (1997). In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. EMBO J. 16, 4826-4838.
2. Amerik, A. Y., Li, S.-J., and Hochstrasser, M. (2000a). Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae. Biol. Chem. 381, 981-992.
3. Amerik, A. Y., Nowak, J., Swaminathan, S., and Hochstrasser, M. (2000b). The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol. Biol. Cell 11, 3365-3380.
4. Ashcroft, M., and Vousden, K. H. (1999). Regulation of p53 stability. Oncogene 18, 7637-7643.
5. Baker, R. T., Tobias, J. T., and Varshavsky, A. (1992). Ubiquitin-specific proteases of Saccharomyces cerevisiae. J. Biol. Chem. 267, 23364-23375.
6. Baxter, B. K., and Craig, E. A. (1998). Isolation of Ubp3, encoding a deubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S. cerevisiae. Curr. Genet. 33, 412-419.
7. Bignell, G. R., Warren, W., Seal, S., Takahashi, M., Raplet, E., Barfoot, R., Green, H., Brown, C., Biggs, P. J., and Lakhani, S. R., et al. (2000). Identification of the familial cylindromatosis tumor-suppressor gene. Nat. Genet. 25, 160-165.
8. Borodovsky, A., Ovaa, H., Nagamalleswari, K., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., and Kessler, B. M. (2002). Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem. Biol. 9, 1149-1159.
9. Brown, G. M., Furlong, R. A., Sargent, C. A., Erickson, R. P., Longepien, G., Mitchell, M., Jones, M. H., Hargreave, T. B., Cooke, H. J., and Affara, N. A. (1998). Characterization of the coding sequence and fine mapping of the human Dffry gene and comparative expression analysis and mapping to the Sxrb interval of the mouse Y chromosome of the Dffry gene. Hum. Mol. Genet. 7, 97-107.
10. Cadavid, A. L. M., Ginzel, A., and Fischer, J. A. (2000). The function of the Drosophila fat facets deubiquitinating enzyme in limiting photoreceptor cell number is intimately associated with endocytosis. Development 127, 1727-1736.
11. Cai, S.-Y., Babbitt, R. W., and Marchesi, V. T. (1999). A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division. Proc. Natl. Acad. Sci. USA 96, 2828-2833.
12. Chen, X., and Fischer, J. A. (2000). In vivo structure/function analysis of the Drosophila fat facets deubiquitinatinge enzyme gene. Genetics 156, 1829-1836.
13. Chen, X., Overstreet, E., Wood, S. A., and Fischer, J. A. (2000). On the conservation of function of the Drosophila Fat facets deubiquitinating enzyme and Fam, its mouse homolog. Dev. Genes Evol. 210, 603-610.
14. Chen, X., Zhang, B., and Fischer, J. A. (2002). A specific protein substrate for a deubiquitinating enzyme: Liquid facets is the substrate of Fat facets. Genes Dev. 16, 289-294.
15. Chung, C. Y., Reddy, T. B. K., Zhou, K., and Firtel, R. A. (1998). A novel, putative MEK kinase controls developmental timing and spatial patterning in Dictyostelium and is regulated by ubiquitin-mediated protein degradation. Genes Dev. 12, 3564-3578.
16. DeSalle, L. M., Latres, E., Lin, D., Graner, D., Montagnoli, A., Baker, R. T., Pagano, M., and Loda, M. (2001). The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein. Oncogene 20, 5538-5542.
17. DiAntonio, A., Haghighi, A. P., Portman, S. L., Lee, J. D., Amaranto, A. M., and Goodman, C. S. (2001). Ubiquitination-dependent mechanisms regulate synaptic growth and function. Nature 412, 449-452.
18. Di Donato, F., Chan, E. K. L., Askanase, A. D., Miranda-Carus, M.-E., and Buyon, J. P. (2001). Interaction between 52 kDa SSA/Ro and deubiquitinating enzyme UnpEL: A clue to function. Intl. J. Biochem. Cell Biol. 33, 924-934.
19. Doelling, J. H., Yan, N., Kurepa, J., Walker, J., and Vierstra, R. D. (2001). The ubiquitin-specific protease Ubp14 is essential for early embryo development in Arabidopsis thaliana. Plant J. 27, 393-405.
20. Dupre, S., and Haguenauer-Tsapis, R. (2001). Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: Crucial role of Doa4p ubiquitin isopeptidase. Mol. Cell. Biol. 21, 4482-4494.
21. Everett, R. D., Meredith, M., Orr, A., Cross, A., Kathoria, M., and Parkinson, J. (1997). A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J. 16, 566-577.
22. Fischer, J. A., and Overstreet, E. (2002). Fat facets does a Highwire act at the synapse. BioEssays 24, 13-16.
23. Fischer, J. A., Leavell, S. K., and Li, Q. (1997). Mutagenesis screens for interacting genes reveal three roles for fat facets during Drosophila eye development. Dev. Gen. 21, 167-174.
24. Fischer-Vize, J. A., Rubin, G. M., and Lehmann, R. (1992). The fat facets gene is required for Drosophila eye and embryo development. Development 116, 985-1000.
25. Frederick, A., Rolfe, M., and Chiu, M. I. (1998). The human Unp locus at 3p21.31 encodes two tissue-selective, cytoplasmic isoforms with deubiquitinating activity that have reduced expression in small cell lung carcinoma cell lines. Oncogene 16, 153-165.
26. Freedman, D. A., Wu, L., and Levine, A. J. (1999). Functions of the Mdm2 oncoprotein. Cell Mol. Life Sci. 55, 96-107.
27. Gnesutta, N., Ceriana, M., Innocenti, M., Mauri, I., Zippel, R., Sturani, E., Borgonovo, B., Berruti, G., and Martegani, E. (2001). Cloning and characterization of mouse UbpY, a deubiquitinating enzyme that interacts with the Ras guanine nucleotide exchange factor Cdc25Mm/Ras-GRF1. J. Biol. Chem. 276, 39448-39454.
28. Gray, D. A., Inazawa, J., Gupta, K., Wong, A., Ueda, R., and Takahashi, T. (1995). Elevated expression of Unph, a proto-oncogene at 3p21.3, in human lung tumors. Oncogene 10, 2179-2183.
29. Gupta, K., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., and Gray, D. A. (1993). Unp, a mouse gene related to the tre oncogene. Oncogene 8, 2307-2310.
30. Gupta, K., Chevrette, M., and Gray, D. A. (1994). The Unp proto-oncogene encodes a nuclear protein. Oncogene 9, 1729-1731.
31. Hadari, T., Warms, J. V., Rose, I. A., and Hershko, A. (1992). A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation. J. Biol. Chem. 267, 719-729.
32. Hegde, A. N., Inokuchi, K., Pei, W., Casadio, A., Ghirardi, M., Chain, D. G., Martin, K. C., Kandel, E. R., and Schwartz, J. H. (1997). Ubiquitin C-terminal hydrolase is an immediate-early gene essential for long-term facilitation in Aplysia. Cell 89, 115-126.
33. Henchoz, S., de Rubertis, F., Pauli, D., and Spierer, P. (1996). The dose of a putative ubiquitin-specific protease affects position-effect variegation in Drosophila melanogaster. Mol. Cell. Biol. 16, 5717-5725.
34. Holzl, H., Kapelari, B., Kellermann, J., Seemuller, E., Sumegi, M., Udvardy, A., Medalia, O., Sperling, J., Muller, S. A., Engel, A., and Baumeister, W. (2000). The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit composition and localization of a deubiquitilating enzyme. J. Cell Biol. 150, 119-130.
35. Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J.-W., Gu, W., Cohen, R. E., and Shi, Y. (2002). Crystal structure of a Ubp-family deubiquitinating enyme in isolation and in complex with ubiquitin aldehyde. Cell 111, 1041-1054.
36. Huang, Y., and Fischer-Vize, J. A. (1996). Undifferentiated cells in the developing Drosophila eye influence facet assembly and require the Fat facets deubiquitinating enzyme. Development 122, 3207-3216.
37. Huang, Y., Baker, R. T., and Fischer-Vize, J. A. (1995). Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene. Science 270, 1828-1831.
38. Isaksson, A., Peverali, F., Kockel, L., Mlodzik, M., and Bohmann, D. (1997). The deubiquitination enzyme Fat facets negatively regulates RTK/Ras/MAPK signalling during Drosophila eye development. Mech. Dev. 68, 59-67.
39. Jaster, R., Zhu, Y., Pless, M., Bhattacharya, S., Mathey-Prevot, B., and D'Andrea, A. D. (1997). Jak2 is required for induction of the murine Dub-1 gene. Mol. Cell. Biol. 17, 3364-3372.
40. Jensen, D. E., and Rauscher, F. J., III. (1999a). Bap1, a candidate tumor suppressor protein that interacts with Brca1. Ann. N.Y. Acad. Sci. 886, 191-194.
41. Jensen, D. E., and Rauscher, F. J., III. (1999b). Defining biochemical functions for the BRCA1 tumor suppressor protein: Analysis of the BRCA1 binding protein BAP1. Cancer Lett. 143, S1, 3-7.
42. Jensen, D. E., Proctor, M., Marquis, S. T., Gardner, H. P., Ha, S. I., Chodosh, L. A., Ishov, A. M., Tommerup, N., Vissing, H., and Sekido, Y., et al. (1998). Bap1: A novel ubiquitin hydrolase which binds to the Brca1 RING finder and enhances Brca1-mediated cell growth suppression. Oncogene 16, 1097-1112.
43. Jones, M. H., Furlong, R. A., Burkin, H., Chalmers, I. J., Brown, G. M., Khwaja, O., and Affara, N. A. (1996). The Drosophila developmental gene fat facets has a human homolog in Xp11.4 which escapes X-inactivation and has related sequences on Yq11.2. Hum. Mol. Genet. 5, 1695-1701.
44. Kahana, A., and Gottschling, D. E. (1999). DOT4 links silencing and cell growth in Saccharomyces cerevisiae. Mol. Cell. Biol. 19, 6608-6620.
45. Kanai-Azuma, M., Mattick, J. S., Kaibuchi, K., and Wood, S. A. (2000). Co-localization of FAM and AF-6, the mammalian homologues of Drosophila Faf and Canoe, in mouse eye development. Mech. Dev. 91, 383-386.
46. Kato, M., Miyazawa, K., and Kitamura, N. (2000). A deubiquitinating enzyme UbpY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP. J. Biol. Chem. 275, 37481-37487.
47. Kurihara, L. J., Semenova, E., Levorse, J. M., and Tilghman, S. M. (2000). Expression and functional analysis of Uch-13 during mouse development. Hum. Mol. Geneta 10, 1963-1970.
48. Kurihara, L. J., Kikuchi, T., Wada, K., and Tilghman, S. M. (2001). Loss of Uch-Lqf and Uch-L3 leads to neurodegeneration, posterior paralysis and dysphagia. Hum. Mol. Genet. 10, 1963-1970.
49. Lam, Y. A., Xu, W., DeMartino, G. N., and Cohen, R. E. (1997a). Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385, 737-740.
50. Lam, Y. A., DeMartino, G. N., Pickart, C. M., and Cohen, R. E. (1997b). Specificity of the ubiquitin isopeptidase in the PA700 regulatory complex of 26S proteasomes. J. Biol. Chem. 272, 28438-28446.
51. Lansbury, P. T.Jr., and Brice, A. (2002). Genetics of Parkinson's disease and biochemical studies of implicated gene products. Curr. Opin. Gen. Dev. 12, 299-306.
52. Lee, J. D., Jee, C., Lee, J. I., Lee, M. H., Lee, M. H., Koo, H.-S., Chung, C. H., and Ahnn, J. (2001). A deubiquitinating enzyme, Uch/CeUbp130, has an essential role in the formation of a functional microtubule-organizing centre (MTOC) during early cleavage in C. elegans. Genes Cells 6, 899-911.
53. Leggett, D. S., Hanna, J., Borodovsky, A., Crosas, B., Schmidt, M., Baker, R. T., Walz, T., Ploegh, H., and Finley, D. (2002). Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10, 495-507.
54. Leroy, E., Boyer, R., Auburger, G., Leube, B., Ulm, G. I., Mezey, E., Harta, G., Brownstein, M. J., Jonnalagada, S., and Chernova, T., et al. (1998). The ubiquitin pathway in Parkinson's disease. Nature 395, 451-452.
55. Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A. Y., Qin, J., and Gu, W. (2002). Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416, 648-653.
56. Li, Q., Hariharan, I. K., Chen, F., Huang, Y., and Fischer, J. A. (1997). Genetic interaction with Rap1 and Ras1 reveal a second function for the fat facets gene in Drosophila eye development. Proc. Natl. Acad. Sci. USA 94, 12515-12520.
57. Li, Z., Na, X., Wang, D., Schoen, S. R., and Messing, E. M. (2002). Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein. J. Biol. Chem. 277, 4656-4662.
58. Lin, H., Keriel, A., Morales, C. R., Bedard, N., Zhao, Q., Hingamp, P., Lefrancois, S., Combaret, L., and Wing, S. S. (2000). Divergent N-terminal sequences target an inducible testis deubiquitinating enzyme to distinct subcellular structures. Mol. Cell. Biol. 20, 6568-6578.
59. Lindsey, D. F., Amerik, A. Y., Deery, W. J., Bishop, J. D., Hochstrasser, M., and Gomer, R. H. (1998). A deubiquitinating enzyme that disassembles free polyubiquitin chains is required for development but not growth in Dictyostelium. J. Biol. Chem. 273, 29178-29187.
60. Liu, L.-Q., Ilaria, R. J., Kingsley, P. D., Iwama, A., van Etten, R. A., Palis, J., and Zhang, D.-E. (1999). A novel ubiquitin-specific protease, Ubp43, cloned from leukemia fusion protein Aml1-Eto-expressing mice, functions in hematopoietic cell differentiation. Mol. Cell. Biol. 19, 3029-3038.
61. Liu, Y., Fallon, L., Lashuel, H. A., Liu, Z., and Lansbury, P. T., Jr. (2002). The Uch-L1 gene encodes two opposing enzymatic activities that affect α-synuclein degradation and Parkinson's disease susceptibility. Cell 111, 209-218.
62. Lockington, R. A., and Kelly, J. M. (2002). The WD40-repeat protein CreC interacts with and stabilizes the deubiquitinating enzyme CreB in vivo in Aspergillus nidulans. Mol. Microbiol. 43, 1173-1182.
63. Mallery, D. L., Vandenberg, C. J., and Hiom, K. (2002). Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquition chains. EMBO J. 21, 6755-6762.
64. Martin, K. A., Poeck, B., Roth, H., Ebens, A. J., Conley Ballard, L., and Zipursky, S. L. (1995). Mutations disrupting neuronal connectivity in the Drosophila visual system. Neuron 14, 229-240.
65. Migone, T.-S., Humbert, M., Rascle, A., Sandan, D., D'Andrea, A. D., and Johnston, J. A. (2001). The deubiquitinating enzyme Dub-2 prolongs cytokine-induced signal transducers and activators of transcription activation and suppresses apoptosis following cytokine withdrawal. Blood 98, 1935-1941.
66. Moazed, D., and Johnson, A. D. (1996). A deubiquitinating enzyme interacts with Sir4 and regulates silencing in S. cerevisiae. Cell 86, 667-677.
67. Moazed, D., Kistler, A., Axelrod, A., Rine, J., and Johnson, A. D. (1997). Silent information regulator protein complexes in Saccharomyces cerevisiae: A SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3. Proc. Natl. Acad. Sci. USA 94, 2186-2191.
68. Montell, D., Rorth, P., and Spradling, A. C. (1992). slow border cells, a locus required for a developmentally regulated cell migration during oogenesis, encodes a Drosophila C/EBP. Cell 71, 51-62.
69. Nakamura, T., Hillova, J., Mariage-Samson, R., Onno, M., Huebner, K., Cannizzaro, L. A., Boghosian-Sell, L., Croce, C. M., and Hill, M. (1992). A novel transcriptional unit of the tre oncogene widely expressed in human cancer cells. Oncogene 7, 733-741.
70. Naviglio, S., Matteucci, C., Matoskova, B., Nagase, T., Nomura, N., Di Fiore, P. P., and Craetta, G. F. (1998). UbpY: A growth-regulated human ubiquitin isopeptidase. EMBO J. 17, 3241-3250.
71. Naze, P., Vuillaume, I., Destee, A., Pasquier, F., and Sablonniere, B. (2002). Mutation analysis and association studies of the ubiquitin carboxy-terminal hydrolase L1 gene in Huntington's disease. Neurosci. Lett. 328, 1-4.
72. Onno, M., Nakamura, T., Hillova, J., and Hill, M. (1993a). Identification of novel sequences in the repertoire of hypervariable TRE17 genes from immortalized nonmalignant and malignant human keratinocytes. Gene 131, 209-215.
73. Onno, M., Nakamura, T., Mariage-Samson, R., Hillova, J., and Hill, M. (1993b). Human TRE17 oncogene is generated from a family of homologous polymorphic sequences by single-base changes. DNA Cell Biol. 12, 107-118.
74. Oren, M. (1999). Regulation of the p53 tumor suppressor protein. J. Biol Chem. 274, 36031-36034.
75. Overstreet, E., Chen, X., Wendland, B., and Fischer, J. A. (2003). Either part of a Drosophila epsin protein, divided after the ENTH domain, functions in endocytosis of Delta in the developing eve. Curr. Biol. 13, 854-860.
76. Pantaleon, M., Kanai-Azuma, M., Mattick, J. S., Kaibuchi, K., Kaye, P. L., and Wood, S. A. (2001). FAM deubiquitylating enzyme is essential for preimplantation mouse embryo development. Mech. Dev. 109, 151-160.
77. Papa, F. R., and Hochstrasser, M. (1993). The yeast doa4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 366, 313-319.
78. Papa, F. R., Amerik, A. Y., and Hochstrasser, M. (1999). Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome. Mol. Biol. Cell 10, 741-756.
79. Park, K. C., Woo, S. K., Yoo, Y. J., Wyndham, A. M., Baker, R. T., and Chung, C. H. (1997). Purification and characterization of Ubp6, a novel ubiquitin protease in Saccharomyces cerevisiae. Arch. Biochem. 347, 78-84.
80. Parks, A. L., Furner, F. R., and Muskavitch, M. A. T. (1995). Relationships between complex Delta expression and the specification of retinal cell fates during Drosophila eye development. Mech. Dev. 50, 201-216.
81. Parks, A. L., Klueg, K. M., Stout, J. R., and Muskavitch, M. A. T. (2000). Ligand endocytosis drives receptor dissociation and activation in the Notch pathway. Development 127, 1373-1385.
82. Poeck, B., Fischer, S., Gunning, D., Zipursky, S. L., and Salecker, I. (2001). Glial cells mediate target layer selection of retinal exons in the developing visual system of Drosophila. Neuron 29, 99-113.
83. Richert, K., Schmidt, H., Gross, T., and Kaufer, F. (2003). The deubiquitinating enzyme Ubp21p of fission yeast stabilizes a mutant form of protein kinase Prp4p. Mol. Genet. Genomics 267, 88-95.
84. Rorth, P., Szabo, K., and Texido, G. (2000). The level of C/EBP protein is critical for cell migration during Drosophila oogenesis and is tightly controlled by regulated degradation. Mol. Cell 6, 23-30.
85. Saigoh, K., Wang, Y. L., Suh, J. G., Yamanishi, T., Sakai, Y., Kiyosawa, H., Harada, T., Ichihara, N., Wakana, S., and Kikuchi, T., et al. (1999). Intragenic deletion in the gene encoding ubiquitn-carboxy-terminal hydrolase in gad mice. Nat. Genet. 23, 47-51.
86. Sherr, C. J., and Webber, J. D. (2000). The ARF/p53 pathway. Curr. Opin. Genet. Dev. 10, 94-99.
87. Shieh, S. Y., Ikeda, M., Taya, Y., and Prives, C. (1997). DNA damage-induced phosphorylation of p53 alleviates inhibition by Mdm2. Cell 91, 325-334.
88. Singer, M. S., Kahana, A. J., Wolf, A. J., Meisinger, L. L., Peterson, S. E., Goggin, C., Mahowald, M., and Gottschling, D. E. (1998). Identification of high copy disruptors of telomeric silencing in Saccharomyces cerevisiae. Genetics 150, 613-632.
89. Swaminathan, S., Amerik, A. Y., and Hochstrasser, M. (1999). The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Mol. Biol. Cell 10, 2583-2594.
90. Taya, S., Yamamoto, T., Kano, K., Kawano, Y., Klwamatsu, A., Tsuchiya, T., Tanaka, K., Kanai-Azuma, M., Wood, S. A., and Mattick, J. S., et al. (1998). The Ras target AF-6 is a substrate of the Fam deubiquitinating enzyme. J. Cell Biol. 142, 1053-1062.
91. Taya, S., Yamamoto, T., Kanai-Azuma, M., Wood, S. A., and Kaibuchi, K. (1999). The deubiquitinating enzyme Fam interacts with and stabilizes β-catenin. Genes Cells 4, 757-767.
92. Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R. I., Koonin, E. V., and Deshaies, R. J. (2002). Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611-615.
93. Weissman, A. M. (2001). Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2, 169-178.
94. Wilkinson, K. D., and Hochstrasser, M. (1998). The deubiquitinating enzymes. In "Ubiquitin and the Biology of the Cell" (J.-M. Peters, J. R. Harris, and D. Finley, Eds.), pp. 99-125. Plenum Press, New York.
95. Wilkinson, K. D., Lee, K. M., Deshpande, S., Duerksen-Hughes, P. J., Boss, J. M., and Pohl, J. (1989). The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase. Science 246, 670-673.
96. Wilkinson, K. D., Tashayev, V. L., O'Connor, L. B., Larsen, C. N., Kasperek, E., and Pickart, C. M. (1995). Metabolism of the polyubiquitin degradation signal: Structure, mechanism, and role of isopeptidase T. Biochemistry 34, 14535-14546.
97. Wood, S. A., Pascoe, W. S., Ru, K., Yamada, T., Hirchenhain, J., Kemler, R., and Mattick, J. S. (1997). Cloning and expression analysis of a novel mouse gene with sequence similarity to the Drosophila fat facets gene. Mech. Dev. 63, 29-38.
98. Wu, Z., Li, Q., Fortini, M., and Fischer, J. A. (1999). Genetic analysis of the role of the Drosophila fat facets gene in the ubiquitin pathway. Dev. Gen. 25, 312-320.
99. Yamazaki, K., Wakasugi, M., Tomita, T., Kikuchi, T., Mukoyama, M., and Ando, K. (1988). Gracile axonal dystrophy (GAD), a new neurological mutant in the mouse. Proc. Soc. Exp. Biol. Med. 187, 209-215.
100. Yao, T., and Cohen, R. E. (2002). A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403-407.
101. Zhu, Y., Carroll, M., Papa, F. R., Hochstrasser, M., and D'Andrea, A. D. (1996a). Dub-1, a deubiquitinating enzyme with growth-suppressing activity. Proc. Natl. Acad. Sci. USA 93, 3275-3279.
102. Zhu, Y., Pless, M., Inhorn, R., Mathey-Prevot, B., and D'Andrea, A. D. (1996b). The murine Dub-1 gene is specificially induced by the be subunit of the interleukin-3 receptor. Mol. Cell. Biol. 16, 4808-4817.
103. Zhu, Y., Lambert, K., Corless, C., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., and D'Andrea, A. D. (1997). Dub-2 is a member of a novel family of cytokine-inducible deubiquitinating enzymes. J. Biol. Chem. 272, 51-57.