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Accession information: Vol. 7; Issue 12; 21 June 2005 Abstract
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Mammalian deubiquitinating enzymes with known function
Paul C. Evans
| Table 1. Mammalian deubiquitinating enzymes with known function | |||
|
Deubiquitinating enzyme |
Function | Target | Refs |
| HAUSP | Apoptosis regulator | p53 | 18, 19 |
| CYLD | Cylindromatosis gene product | NEMO | 15, 16, 17, 62 |
| DUB-1 | B-cell survival (induced by IL-3) | ? | 26, 28 |
| DUB-2 | T-cell survival (induced by IL-2) | ? | 27, 29 |
| BAP-1 | Mammary gland development | ? | 22, 23, 101 |
| UCH-L1 | Gracile axonal dystrophy gene product | ? | 21 |
| Usp14 | Synaptic transmission | ? | 20 |
| Abbreviations: BAP, BRCA1-associated protein; CYLD, cylindromatosis gene; DUB, deubiquitinating enzyme; HAUSP, herpesvirus-associated ubiquitin-specific protease; IL, interleukin; NEMO, NF-kB essential modifier; UCH, ubiquitin C-terminal hydrolase; Usp, ubiquitin-specific processing protease. | |||
| References cited
in Table 1
15 Trompouki, E. et al. (2003) CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 424, 793-796, PubMed 16 Brummelkamp, T.R. et al. (2003) Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature 424, 797-801, PubMed 17 Kovalenko, A. et al. (2003) The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 424, 801-805, PubMed 18 Cummins, J.M. and Vogelstein, B. (2004) HAUSP is required for p53 destabilization. Cell Cycle 3, 689-692, PubMed 19 Cummins, J.M. et al. (2004) Tumour suppression: disruption of HAUSP gene stabilizes p53. Nature 428, 1 p following 486, PubMed 20 Wilson, S.M. et al. (2002) Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease. Nat Genet 32, 420-425, PubMed 21 Saigoh, K. et al. (1999) Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice. Nat Genet 23, 47-51, PubMed 22 Jensen, D.E. et al. (1998) BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression. Oncogene 16, 1097-1112, PubMed 23 Jensen, D.E. and Rauscher, F.J., 3rd (1999) Defining biochemical functions for the BRCA1 tumor suppressor protein: analysis of the BRCA1 binding protein BAP1. Cancer Lett 143 Suppl 1, S13-17, PubMed 26 Zhu, Y. et al. (1996) DUB-1, a deubiquitinating enzyme with growth-suppressing activity. Proc Natl Acad Sci U S A 93, 3275-3279, PubMed 27 Zhu, Y. et al. (1997) DUB-2 is a member of a novel family of cytokine-inducible deubiquitinating enzymes. J Biol Chem 272, 51-57, PubMed 28 Baek, K.H. et al. (2004) DUB-1A, a novel deubiquitinating enzyme subfamily member, is polyubiquitinated and cytokine-inducible in B-lymphocytes. J Biol Chem 279, 2368-2376, PubMed 29 Baek, K.H. et al. (2001) DUB-2A, a new member of the DUB subfamily of hematopoietic deubiquitinating enzymes. Blood 98, 636-642, PubMed 62 Bignell, G.R. et al. (2000) Identification of the familial cylindromatosis tumour-suppressor gene. Nat Genet 25, 160-165, PubMed 101 Jensen, D.E. and Rauscher, F.J., 3rd (1999) BAP1, a candidate tumor suppressor protein that interacts with BRCA1. Ann N Y Acad Sci 886, 191-194, PubMed |
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