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Volumn 125, Issue 2, 2012, Pages 277-286

Cellular functions of the DUBs

Author keywords

[No Author keywords available]

Indexed keywords

DEUBIQUITINASE; ENZYME; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEINASE; SMAD PROTEIN; SMALL INTERFERING RNA; TRANSFORMING GROWTH FACTOR BETA; UBIQUITIN; UBIQUITIN SPECIFIC PROTEASE; UNCLASSIFIED DRUG; WNT PROTEIN;

EID: 84858119736     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.090985     Document Type: Note
Times cited : (176)

References (139)
  • 1
    • 33747375410 scopus 로고    scopus 로고
    • Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo
    • Agromayor, M. and Martin-Serrano, J. (2006). Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo. J. Biol. Chem. 281, 1374-1387.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1374-1387
    • Agromayor, M.1    Martin-Serrano, J.2
  • 2
    • 80054079071 scopus 로고    scopus 로고
    • Assembly and disassembly of the ESCRT-III membrane scission complex
    • Alonso, Y., Adell, M. and Teis, D. (2011). Assembly and disassembly of the ESCRT-III membrane scission complex. FEBS Lett. 585, 3191-3196.
    • (2011) FEBS Lett , vol.585 , pp. 3191-3196
    • Alonso, Y.1    Adell, M.2    Teis, D.3
  • 3
    • 0033786796 scopus 로고    scopus 로고
    • The DoA4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways
    • Amerik, A. Y., Nowak, J., Swaminathan, S. and Hochstrasser, M. (2000). The DoA4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol. Biol. Cell 11, 3365-3380.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3365-3380
    • Amerik, A.Y.1    Nowak, J.2    Swaminathan, S.3    Hochstrasser, M.4
  • 4
    • 33645714061 scopus 로고    scopus 로고
    • The KLH12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation
    • Angers, S., Thorpe, C. J., Bischele, T. L., Goldenberg, S. J., Zheng, N., MacCoss, M. J. and Moon, R. T. (2006). The KLH12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation. Nat. Cell Biol. 8, 348-357.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 348-357
    • Angers, S.1    Thorpe, C.J.2    Bischele, T.L.3    Goldenberg, S.J.4    Zheng, N.5    MacCoss, M.J.6    Moon, R.T.7
  • 5
    • 79959847254 scopus 로고    scopus 로고
    • The role of deubiquitinating enzymes in chromatin regulation
    • Atanassov, B. S., Koutelou, E. and Dent, S. Y. (2011). The role of deubiquitinating enzymes in chromatin regulation. FEBS Lett. 585, 2016-2023.
    • (2011) FEBS Lett , vol.585 , pp. 2016-2023
    • Atanassov, B.S.1    Koutelou, E.2    Dent, S.Y.3
  • 6
    • 80355148474 scopus 로고    scopus 로고
    • Role of ubiquitylation and USP8-dependent deubiquitylation in the endocytosis and lysosomal targeting of plasma membrane KCa3.1.
    • Balut, C. M., Loch, C. M. and Devor, D. C. (2011). Role of ubiquitylation and USP8-dependent deubiquitylation in the endocytosis and lysosomal targeting of plasma membrane KCa3.1. FASEB J. 25, 3938-3948.
    • (2011) FASEB J. , vol.25 , pp. 3938-3948
    • Balut, C.M.1    Loch, C.M.2    Devor, D.C.3
  • 7
    • 80052697814 scopus 로고    scopus 로고
    • The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks
    • Bekker-Jensen, S. and Mailand, N. (2011). The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks. FEBS Lett. 585, 2914-2919.
    • (2011) FEBS Lett , vol.585 , pp. 2914-2919
    • Bekker-Jensen, S.1    Mailand, N.2
  • 8
    • 78549264851 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP8 promotes trafficking and degradation of the chemokine receptor 4 at the sorting endosome
    • Berlin, I., Higginbotham, K. M., Dise, R. S., Sierra, M. I. and Nash, P. D. (2010a). The deubiquitinating enzyme USP8 promotes trafficking and degradation of the chemokine receptor 4 at the sorting endosome. J. Biol. Chem. 285, 37895-37908.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37895-37908
    • Berlin, I.1    Higginbotham, K.M.2    Dise, R.S.3    Sierra, M.I.4    Nash, P.D.5
  • 9
    • 78049404751 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor ubiquitination and trafficking by the USP8. STAM complex
    • Berlin, I., Schwartz, H. and Nash, P. D. (2010b). Regulation of epidermal growth factor receptor ubiquitination and trafficking by the USP8.STAM complex. J. Biol. Chem. 285, 34909-34921.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34909-34921
    • Berlin, I.1    Schwartz, H.2    Nash, P.D.3
  • 10
    • 67649556158 scopus 로고    scopus 로고
    • The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization
    • Berthouze, M., Venkataramanan, V., Li, Y. and Shenoy, S. K. (2009). The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization. EMBO J. 28, 1684-1696.
    • (2009) EMBO J , vol.28 , pp. 1684-1696
    • Berthouze, M.1    Venkataramanan, V.2    Li, Y.3    Shenoy, S.K.4
  • 11
    • 77953902511 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP10 regulates the endocytic recycling of CFTR in airway epithelial cells
    • Bomberger, J. M., Barnaby, R. L. and Stanton, B. A. (2010). The deubiquitinating enzyme USP10 regulates the endocytic recycling of CFTR in airway epithelial cells. Channels (Austin) 4, 150-154.
    • (2010) Channels (Austin) , vol.4 , pp. 150-154
    • Bomberger, J.M.1    Barnaby, R.L.2    Stanton, B.A.3
  • 13
    • 33646171781 scopus 로고    scopus 로고
    • Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII
    • Bowers, K., Piper, S. C., Edeling, M. A., Gray, S. R., Owen, D. J., Lehner, P. J. and Luzio, J. P. (2006). Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII. J. Biol. Chem. 281, 5094-5105.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5094-5105
    • Bowers, K.1    Piper, S.C.2    Edeling, M.A.3    Gray, S.R.4    Owen, D.J.5    Lehner, P.J.6    Luzio, J.P.7
  • 14
    • 77955417276 scopus 로고    scopus 로고
    • Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne
    • Bremm, A., Freund, S. M. and Komander, D. (2010). Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. Nat. Struct. Mol. Biol. 17, 939-947.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 939-947
    • Bremm, A.1    Freund, S.M.2    Komander, D.3
  • 15
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB
    • Brummelkamp, T. R., Nijman, S. M., Dirac, A. M. and Bernards, R. (2003). Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature 424, 797-801.
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 16
    • 69949173205 scopus 로고    scopus 로고
    • Deubiquitinase activities required for hepatocyte growth factor-induced scattering of epithelial cells
    • Buus, R., Faronato, M., Hammond, D. E., Urbe, S. and Clague, M. J. (2009). Deubiquitinase activities required for hepatocyte growth factor-induced scattering of epithelial cells. Curr. Biol. 19, 1463-1466.
    • (2009) Curr. Biol. , vol.19 , pp. 1463-1466
    • Buus, R.1    Faronato, M.2    Hammond, D.E.3    Urbe, S.4    Clague, M.J.5
  • 17
    • 34347385894 scopus 로고    scopus 로고
    • Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery
    • Carlton, J. G. and Martin-Serrano, J. (2007). Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science 316, 1908-1912.
    • (2007) Science , vol.316 , pp. 1908-1912
    • Carlton, J.G.1    Martin-Serrano, J.2
  • 18
    • 65249083913 scopus 로고    scopus 로고
    • Ubiquitin in NF-kappaB signaling
    • Chiu, Y. H., Zhao, M. and Chen, Z. J. (2009). Ubiquitin in NF-kappaB signaling. Chem. Rev. 109, 1549-1560.
    • (2009) Chem. Rev. , vol.109 , pp. 1549-1560
    • Chiu, Y.H.1    Zhao, M.2    Chen, Z.J.3
  • 19
    • 33750302074 scopus 로고    scopus 로고
    • Endocytosis: the DUB version
    • Clague, M. J. and Urbe, S. (2006). Endocytosis: the DUB version. Trends Cell Biol. 16, 551-559.
    • (2006) Trends Cell Biol , vol.16 , pp. 551-559
    • Clague, M.J.1    Urbe, S.2
  • 20
    • 78650100616 scopus 로고    scopus 로고
    • Ubiquitin: same molecule, different degradation pathways
    • Clague, M. J. and Urbe, S. (2010). Ubiquitin: same molecule, different degradation pathways. Cell 143, 682-685.
    • (2010) Cell , vol.143 , pp. 682-685
    • Clague, M.J.1    Urbe, S.2
  • 21
    • 36749082959 scopus 로고    scopus 로고
    • A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway
    • Cohn, M. A., Kowal, P., Yang, K., Haas, W., Huang, T. T., Gygi, S. P. and D'Andrea, A. D. (2007). A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway. Mol. Cell 28, 786-797.
    • (2007) Mol. Cell , vol.28 , pp. 786-797
    • Cohn, M.A.1    Kowal, P.2    Yang, K.3    Haas, W.4    Huang, T.T.5    Gygi, S.P.6    D'Andrea, A.D.7
  • 22
    • 62649104153 scopus 로고    scopus 로고
    • K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISCassociated Brcc36 and proteasomal Poh1
    • Cooper, E. M., Cutcliffe, C., Kristiansen, T. Z., Pandey, A., Pickart, C. M. and Cohen, R. E. (2009). K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISCassociated Brcc36 and proteasomal Poh1. EMBO J. 28, 621-631.
    • (2009) EMBO J , vol.28 , pp. 621-631
    • Cooper, E.M.1    Cutcliffe, C.2    Kristiansen, T.Z.3    Pandey, A.4    Pickart, C.M.5    Cohen, R.E.6
  • 23
    • 85047690484 scopus 로고    scopus 로고
    • Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation
    • Curcio-Morelli, C., Zavacki, A. M., Christofollete, M., Gereben, B., de Freitas, B. C., Harney, J. W., Li, Z., Wu, G. and Bianco, A. C. (2003). Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation. J. Clin. Invest. 112, 189-196.
    • (2003) J. Clin. Invest. , vol.112 , pp. 189-196
    • Curcio-Morelli, C.1    Zavacki, A.M.2    Christofollete, M.3    Gereben, B.4    de Freitas, B.C.5    Harney, J.W.6    Li, Z.7    Wu, G.8    Bianco, A.C.9
  • 24
    • 79952101583 scopus 로고    scopus 로고
    • Early phase TGFbeta receptor signalling dynamics stabilised by the deubiquitinase UCH37 promotes cell migratory responses
    • Cutts, A. J., Soond, S. M., Powell, S. and Chantry, A. (2011). Early phase TGFbeta receptor signalling dynamics stabilised by the deubiquitinase UCH37 promotes cell migratory responses. Int. J. Biochem. Cell Biol. 43, 604-612.
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 604-612
    • Cutts, A.J.1    Soond, S.M.2    Powell, S.3    Chantry, A.4
  • 25
    • 38849110179 scopus 로고    scopus 로고
    • Targeting ubiquitin specific proteases for drug discovery
    • Daviet, L. and Colland, F. (2008). Targeting ubiquitin specific proteases for drug discovery. Biochimie 90, 270-283.
    • (2008) Biochimie , vol.90 , pp. 270-283
    • Daviet, L.1    Colland, F.2
  • 26
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains-from structures to functions
    • Dikic, I., Wakatsuki, S. and Walters, K. J. (2009). Ubiquitin-binding domains-from structures to functions. Nat. Rev. Mol. Cell Biol. 10, 659-671.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 27
    • 79955985329 scopus 로고    scopus 로고
    • USP10 deubiquitylates the histone variant H2A, Z and both are required for androgen receptor-mediated gene activation
    • Draker, R., Sarcinella, E. and Cheung, P. (2011). USP10 deubiquitylates the histone variant H2A.Z and both are required for androgen receptor-mediated gene activation. Nucleic Acids Res. 39, 3529-3542.
    • (2011) Nucleic Acids Res , vol.39 , pp. 3529-3542
    • Draker, R.1    Sarcinella, E.2    Cheung, P.3
  • 28
    • 78049510229 scopus 로고    scopus 로고
    • DNMT1 stability is regulated by proteins coordinating deubiquitination and acetylation-driven ubiquitination
    • Du, Z., Song, J., Wang, Y., Zhao, Y., Guda, K., Yang, S., Kao, H. Y., Xu, Y., Willis, J., Markowitz, S. D. et al. (2010). DNMT1 stability is regulated by proteins coordinating deubiquitination and acetylation-driven ubiquitination. Sci. Signal. 3, ra80.
    • (2010) Sci. Signal. , vol.3
    • Du, Z.1    Song, J.2    Wang, Y.3    Zhao, Y.4    Guda, K.5    Yang, S.6    Kao, H.Y.7    Xu, Y.8    Willis, J.9    Markowitz, S.D.10
  • 29
    • 33646147146 scopus 로고    scopus 로고
    • Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules
    • Duncan, L. M., Piper, S., Dodd, R. B., Saville, M. K., Sanderson, C. M., Luzio, J. P. and Lehner, P. J. (2006). Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules. EMBO J. 25, 1635-1645.
    • (2006) EMBO J , vol.25 , pp. 1635-1645
    • Duncan, L.M.1    Piper, S.2    Dodd, R.B.3    Saville, M.K.4    Sanderson, C.M.5    Luzio, J.P.6    Lehner, P.J.7
  • 31
    • 0034955239 scopus 로고    scopus 로고
    • Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase
    • 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.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4482-4494
    • Dupre, S.1    Haguenauer-Tsapis, R.2
  • 32
    • 77649274212 scopus 로고    scopus 로고
    • Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction
    • Eden, E. R., White, I. J., Tsapara, A. and Futter, C. E. (2010). Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction. Nat. Cell Biol. 12, 267-272.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 267-272
    • Eden, E.R.1    White, I.J.2    Tsapara, A.3    Futter, C.E.4
  • 33
    • 70349778618 scopus 로고    scopus 로고
    • The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER
    • Ernst, R., Mueller, B., Ploegh, H. L. and Schlieker, C. (2009). The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol. Cell 36, 28-38.
    • (2009) Mol. Cell , vol.36 , pp. 28-38
    • Ernst, R.1    Mueller, B.2    Ploegh, H.L.3    Schlieker, C.4
  • 36
    • 77957260099 scopus 로고    scopus 로고
    • The Lys63-specific deubiquitinating enzyme BRCC36 is regulated by two scaffold proteins localizing in different subcellular compartments
    • Feng, L., Wang, J. and Chen, J. (2010). The Lys63-specific deubiquitinating enzyme BRCC36 is regulated by two scaffold proteins localizing in different subcellular compartments. J. Biol. Chem. 285, 30982-30988.
    • (2010) J. Biol. Chem. , vol.285 , pp. 30982-30988
    • Feng, L.1    Wang, J.2    Chen, J.3
  • 37
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. (2009). Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 38
    • 80052694448 scopus 로고    scopus 로고
    • Dynamic regulation of PCNA ubiquitylation/deubiquitylation
    • Fox, J. T., Lee, K. Y. and Myung, K. (2011). Dynamic regulation of PCNA ubiquitylation/deubiquitylation. FEBS Lett. 585, 2780-2785.
    • (2011) FEBS Lett , vol.585 , pp. 2780-2785
    • Fox, J.T.1    Lee, K.Y.2    Myung, K.3
  • 39
    • 79953164696 scopus 로고    scopus 로고
    • Gene expression control by protein deubiquitinases
    • Frappier, L. and Verrijzer, C. P. (2011). Gene expression control by protein deubiquitinases. Curr. Opin. Genet. Dev. 21, 207-213.
    • (2011) Curr. Opin. Genet. Dev. , vol.21 , pp. 207-213
    • Frappier, L.1    Verrijzer, C.P.2
  • 40
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J. M. and Haguenauer-Tsapis, R. (1997). Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16, 5847-5854.
    • (1997) EMBO J , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 41
    • 77955172368 scopus 로고    scopus 로고
    • Autophagy negatively regulates Wnt signaling by promoting Dishevelled degradation
    • Gao, C., Cao, W., Bao, L., Zuo, W., Xie, G., Cai, T., Fu, W., Zhang, J., Wu, W., Zhang, X. et al. (2010). Autophagy negatively regulates Wnt signaling by promoting Dishevelled degradation. Nat. Cell Biol. 12, 781-790.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 781-790
    • Gao, C.1    Cao, W.2    Bao, L.3    Zuo, W.4    Xie, G.5    Cai, T.6    Fu, W.7    Zhang, J.8    Wu, W.9    Zhang, X.10
  • 42
    • 21744433162 scopus 로고    scopus 로고
    • Ubp10/Dot4p regulates the persistence of ubiquitinated histone H2B: distinct roles in telomeric silencing and general chromatin
    • Gardner, R. G., Nelson, Z. W. and Gottschling, D. E. (2005). Ubp10/Dot4p regulates the persistence of ubiquitinated histone H2B: distinct roles in telomeric silencing and general chromatin. Mol. Cell. Biol. 25, 6123-6139.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6123-6139
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 43
    • 79956027089 scopus 로고    scopus 로고
    • USP1 deubiquitinase maintains phosphorylated CHK1 by limiting its DDB1-dependent degradation
    • Guervilly, J. H., Renaud, E., Takata, M. and Rosselli, F. (2011). USP1 deubiquitinase maintains phosphorylated CHK1 by limiting its DDB1-dependent degradation. Hum. Mol. Genet. 20, 2171-2181.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2171-2181
    • Guervilly, J.H.1    Renaud, E.2    Takata, M.3    Rosselli, F.4
  • 44
    • 38149054804 scopus 로고    scopus 로고
    • Axin and GSK-β control Smad3 protein stability and modulate TGF-β signaling
    • Guo, X., Ramirez, A., Waddell, D. S., Li, Z., Liu, X. and Wang, X.-F. (2008). Axin and GSK-β control Smad3 protein stability and modulate TGF-β signaling. Genes Dev. 22, 106-120.
    • (2008) Genes Dev , vol.22 , pp. 106-120
    • Guo, X.1    Ramirez, A.2    Waddell, D.S.3    Li, Z.4    Liu, X.5    Wang, X.-F.6
  • 45
    • 78650915537 scopus 로고    scopus 로고
    • Deubiquitinases in the regulation of NF-kB signaling
    • Harhaj, E. W. and Dixit, V. M. (2011). Deubiquitinases in the regulation of NF-kB signaling. Cell Res. 21, 22-39.
    • (2011) Cell Res , vol.21 , pp. 22-39
    • Harhaj, E.W.1    Dixit, V.M.2
  • 46
    • 70350514475 scopus 로고    scopus 로고
    • Endosomal deubiquitinating enzymes control ubiquitination and down-regulation of proteaseactivated receptor 2
    • Hasdemir, B., Murphy, J. E., Cottrell, G. S. and Bunnett, N. W. (2009). Endosomal deubiquitinating enzymes control ubiquitination and down-regulation of proteaseactivated receptor 2. J. Biol. Chem. 284, 28453-28466.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28453-28466
    • Hasdemir, B.1    Murphy, J.E.2    Cottrell, G.S.3    Bunnett, N.W.4
  • 48
    • 63749105896 scopus 로고    scopus 로고
    • Mechanism of TGF-beta signaling to growth arrest, apoptosis, and epithelial-mesenchymal transition
    • Heldin, C. H., Landstrom, M. and Moustakas, A. (2009). Mechanism of TGF-beta signaling to growth arrest, apoptosis, and epithelial-mesenchymal transition. Curr. Opin. Cell Biol. 21, 166-176.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 166-176
    • Heldin, C.H.1    Landstrom, M.2    Moustakas, A.3
  • 51
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke, L. and Dunn, R. (2003). Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19, 141-172.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 52
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • Huang, F., Kirkpatrick, D., Jiang, X., Gygi, S. and Sorkin, A. (2006a). Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol. Cell 21, 737-748.
    • (2006) Mol. Cell , vol.21 , pp. 737-748
    • Huang, F.1    Kirkpatrick, D.2    Jiang, X.3    Gygi, S.4    Sorkin, A.5
  • 54
    • 68149160205 scopus 로고    scopus 로고
    • The COP9 signalosome mediates beta-catenin degradation by deneddylation and blocks adenomatous polyposis coli destruction via USP15
    • Huang, X., Langelotz, C., Hetfeld-Pechoc, B. K., Schwenk, W. and Dubiel, W. (2009). The COP9 signalosome mediates beta-catenin degradation by deneddylation and blocks adenomatous polyposis coli destruction via USP15. J. Mol. Biol. 391, 691-702.
    • (2009) J. Mol. Biol. , vol.391 , pp. 691-702
    • Huang, X.1    Langelotz, C.2    Hetfeld-Pechoc, B.K.3    Schwenk, W.4    Dubiel, W.5
  • 55
    • 36749010218 scopus 로고    scopus 로고
    • The age of crosstalk: phosphorylation, ubiquitination, and beyond
    • Hunter, T. (2007). The age of crosstalk: phosphorylation, ubiquitination, and beyond. Mol. Cell 28, 730-738.
    • (2007) Mol. Cell , vol.28 , pp. 730-738
    • Hunter, T.1
  • 56
    • 80051485763 scopus 로고    scopus 로고
    • Nipped in the bud: how the AMSH MIT domain helps deubiquitinate lysosome bound cargo
    • Hurley, J. H. (2011). Nipped in the bud: how the AMSH MIT domain helps deubiquitinate lysosome bound cargo. Structure 19, 1033-1035.
    • (2011) Structure , vol.19 , pp. 1033-1035
    • Hurley, J.H.1
  • 57
    • 37849000664 scopus 로고    scopus 로고
    • MIT domainia
    • Hurley, J. H. and Yang, D. (2008). MIT domainia. Dev. Cell 14, 6-8.
    • (2008) Dev. Cell , vol.14 , pp. 6-8
    • Hurley, J.H.1    Yang, D.2
  • 59
    • 55449107515 scopus 로고    scopus 로고
    • Regulation of TGF-beta family signaling by E3 ubiquitin ligases
    • Inoue, Y. and Imamura, T. (2008). Regulation of TGF-beta family signaling by E3 ubiquitin ligases. Cancer Sci. 99, 2107-2112.
    • (2008) Cancer Sci , vol.99 , pp. 2107-2112
    • Inoue, Y.1    Imamura, T.2
  • 61
    • 0035422199 scopus 로고    scopus 로고
    • Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads
    • Itoh, F., Asao, H., Sugamura, K., Heldin, C. H., ten Dijke, P. and Itoh, S. (2001). Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads. EMBO J. 20, 4132-4142.
    • (2001) EMBO J , vol.20 , pp. 4132-4142
    • Itoh, F.1    Asao, H.2    Sugamura, K.3    Heldin, C.H.4    ten Dijke, P.5    Itoh, S.6
  • 62
    • 35548986309 scopus 로고    scopus 로고
    • Regulation of cell cycle progression and gene expression by H2A deubiquitination
    • Joo, H. Y., Zhai, L., Yang, C., Nie, S., Erdjument-Bromage, H., Tempst, P., Chang, C. and Wang, H. (2007). Regulation of cell cycle progression and gene expression by H2A deubiquitination. Nature 449, 1068-1072.
    • (2007) Nature , vol.449 , pp. 1068-1072
    • Joo, H.Y.1    Zhai, L.2    Yang, C.3    Nie, S.4    Erdjument-Bromage, H.5    Tempst, P.6    Chang, C.7    Wang, H.8
  • 65
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • Komander, D., Clague, M. J. and Urbe, S. (2009a). Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 10, 550-563.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 66
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent Lys63-linked and linear polyubiquitin chains
    • Komander, D., Reyes-Turcu, F. J. D. F. L., Odenwaelder, P., Wilkinson, K. D. and Barford, D. (2009b). Molecular discrimination of structurally equivalent Lys63-linked and linear polyubiquitin chains. EMBO Rep. 10, 466-473.
    • (2009) EMBO Rep , vol.10 , pp. 466-473
    • Komander, D.1    Reyes-Turcu, F.2    Licchesi, J.D.3    Odenwaelder, P.4    Wilkinson, K.D.5    Barford, D.6
  • 67
    • 77957893483 scopus 로고    scopus 로고
    • A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity
    • Kouranti, I., McLean, J. R., Feoktistova, A., Liang, P., Johnson, A. E., Roberts-Galbraith, R. H. and Gould, K. L. (2010). A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity. PLoS Biol. 8, e1000471.
    • (2010) PLoS Biol , vol.8
    • Kouranti, I.1    McLean, J.R.2    Feoktistova, A.3    Liang, P.4    Johnson, A.E.5    Roberts-Galbraith, R.H.6    Gould, K.L.7
  • 68
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • Kovalenko, A., Chable-Bessia, C., Cantarella, G., Israel, A., Wallach, D. and Courtois, G. (2003). The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 424, 801-805.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israel, A.4    Wallach, D.5    Courtois, G.6
  • 69
    • 79251554350 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP-46 negatively regulates the degradation of glutamate receptors to control their abundance in the ventral nerve cord of Caenorhabditis elegans
    • Kowalski, J. R., Dahlberg, C. L. and Juo, P. (2011). The deubiquitinating enzyme USP-46 negatively regulates the degradation of glutamate receptors to control their abundance in the ventral nerve cord of Caenorhabditis elegans. J. Neurosci. 31, 1341-1354.
    • (2011) J. Neurosci. , vol.31 , pp. 1341-1354
    • Kowalski, J.R.1    Dahlberg, C.L.2    Juo, P.3
  • 70
    • 79952280797 scopus 로고    scopus 로고
    • The Machado-Joseph disease deubiquitylase ATX-3 couples longevity and proteostasis
    • Kuhlbrodt, K., Janiesch, P. C., Kevei, E., Segref, A., Barikbin, R. and Hoppe, T. (2011). The Machado-Joseph disease deubiquitylase ATX-3 couples longevity and proteostasis. Nat. Cell Biol. 13, 273-281.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 273-281
    • Kuhlbrodt, K.1    Janiesch, P.C.2    Kevei, E.3    Segref, A.4    Barikbin, R.5    Hoppe, T.6
  • 71
    • 80052597874 scopus 로고    scopus 로고
    • The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements
    • Lang, G., Bonnet, J., Umlauf, D., Karmodiya, K., Koffler, J., Stierle, M., Devys, D. and Tora, L. (2011). The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements. Mol. Cell. Biol. 31, 3734-3744.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3734-3744
    • Lang, G.1    Bonnet, J.2    Umlauf, D.3    Karmodiya, K.4    Koffler, J.5    Stierle, M.6    Devys, D.7    Tora, L.8
  • 72
    • 65649128660 scopus 로고    scopus 로고
    • K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway
    • Lauwers, E., Jacob, C. and Andre, B. (2009). K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J. Cell Biol. 185, 493-502.
    • (2009) J. Cell Biol. , vol.185 , pp. 493-502
    • Lauwers, E.1    Jacob, C.2    Andre, B.3
  • 74
    • 77951210668 scopus 로고    scopus 로고
    • Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear antigen (PCNA) through Its interactions with PCNA and USP1
    • Lee, K. Y., Yang, K., Cohn, M. A., Sikdar, N., D'Andrea, A. D. and Myung, K. (2010b). Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear antigen (PCNA) through Its interactions with PCNA and USP1. J. Biol. Chem. 285, 10362-10369.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10362-10369
    • Lee, K.Y.1    Yang, K.2    Cohn, M.A.3    Sikdar, N.4    D'Andrea, A.D.5    Myung, K.6
  • 75
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • 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.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 76
    • 80053501671 scopus 로고    scopus 로고
    • Beclin1 controls the levels of p53 by regulating the deubiquitination qctivity of USP10 and USP13
    • Liu, J., Xia, H., Kim, M., Xu, L., Li, Y., Zhang, L., Cai, Y., Norberg, H. V., Zhang, T., Furuya, T. et al. (2011). Beclin1 controls the levels of p53 by regulating the deubiquitination qctivity of USP10 and USP13. Cell 147, 223-234.
    • (2011) Cell , vol.147 , pp. 223-234
    • Liu, J.1    Xia, H.2    Kim, M.3    Xu, L.4    Li, Y.5    Zhang, L.6    Cai, Y.7    Norberg, H.V.8    Zhang, T.9    Furuya, T.10
  • 78
    • 77955419051 scopus 로고    scopus 로고
    • Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor
    • Maertens, G. N., El Messaoudi-Aubert, S., Elderkin, S., Hiom, K. and Peters, G. (2010). Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor. EMBO J. 29, 2553-2565.
    • (2010) EMBO J , vol.29 , pp. 2553-2565
    • Maertens, G.N.1    El Messaoudi-Aubert, S.2    Elderkin, S.3    Hiom, K.4    Peters, G.5
  • 80
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • McCullough, J., Clague, M. J. and Urbe, S. (2004). AMSH is an endosome-associated ubiquitin isopeptidase. J. Cell Biol. 166, 487-492.
    • (2004) J. Cell Biol. , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 81
    • 30944464589 scopus 로고    scopus 로고
    • Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery
    • McCullough, J., Row, P. E., Lorenzo, O., Doherty, M., Beynon, R., Clague, M. J. and Urbe, S. (2006). Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery. Curr. Biol. 16, 160-165.
    • (2006) Curr. Biol. , vol.16 , pp. 160-165
    • McCullough, J.1    Row, P.E.2    Lorenzo, O.3    Doherty, M.4    Beynon, R.5    Clague, M.J.6    Urbe, S.7
  • 82
    • 69449086077 scopus 로고    scopus 로고
    • No strings attached: the ESCRT machinery in viral budding and cytokinesis
    • McDonald, B. and Martin-Serrano, J. (2009). No strings attached: the ESCRT machinery in viral budding and cytokinesis. J. Cell Sci. 122, 2167-2177.
    • (2009) J. Cell Sci. , vol.122 , pp. 2167-2177
    • McDonald, B.1    Martin-Serrano, J.2
  • 83
    • 27644438783 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes
    • Mizuno, E., Iura, T., Mukai, A., Yoshimori, T., Kitamura, N. and Komada, M. (2005). Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes. Mol. Biol. Cell 16, 5163-5174.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5163-5174
    • Mizuno, E.1    Iura, T.2    Mukai, A.3    Yoshimori, T.4    Kitamura, N.5    Komada, M.6
  • 84
    • 33745754789 scopus 로고    scopus 로고
    • A Deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes
    • Mizuno, E., Kobayashi, K., Yamamoto, A., Kitamura, N. and Komada, M. (2006). A Deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes. Traffic 7, 1017-10131.
    • (2006) Traffic , vol.7 , pp. 1017-10131
    • Mizuno, E.1    Kobayashi, K.2    Yamamoto, A.3    Kitamura, N.4    Komada, M.5
  • 85
    • 34948911522 scopus 로고    scopus 로고
    • Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
    • Morita, E., Sandrin, V., Chung, H. Y., Morham, S. G., Gygi, S. P., Rodesch, C. K. and Sundquist, W. I. (2007). Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J. 26, 4215-4227.
    • (2007) EMBO J , vol.26 , pp. 4215-4227
    • Morita, E.1    Sandrin, V.2    Chung, H.Y.3    Morham, S.G.4    Gygi, S.P.5    Rodesch, C.K.6    Sundquist, W.I.7
  • 86
    • 34547107878 scopus 로고    scopus 로고
    • A proteomic analysis of ataxia telangiectasia-mutated (ATM)/ATMRad3-related (ATR) substrates identifies the ubiquitin-proteasome system as a regulator for DNA damage checkpoints
    • Mu, J. J., Wang, Y., Luo, H., Leng, M., Zhang, J., Yang, T., Besusso, D., Jung, S. Y. and Qin, J. (2007). A proteomic analysis of ataxia telangiectasia-mutated (ATM)/ATMRad3-related (ATR) substrates identifies the ubiquitin-proteasome system as a regulator for DNA damage checkpoints. J. Biol. Chem. 282, 17330-17334.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17330-17334
    • Mu, J.J.1    Wang, Y.2    Luo, H.3    Leng, M.4    Zhang, J.5    Yang, T.6    Besusso, D.7    Jung, S.Y.8    Qin, J.9
  • 87
    • 44449130420 scopus 로고    scopus 로고
    • Dynamic regulation of ubiquitylation and deubiquitylation at the central spindle during cytokinesis
    • Mukai, A., Mizuno, E., Kobayashi, K., Matsumoto, M., Nakayama, K.I., Kitamura, N. and Komada, M. (2008). Dynamic regulation of ubiquitylation and deubiquitylation at the central spindle during cytokinesis. J. Cell Sci. 121, 1325-1333.
    • (2008) J. Cell Sci. , vol.121 , pp. 1325-1333
    • Mukai, A.1    Mizuno, E.2    Kobayashi, K.3    Matsumoto, M.4    Nakayama, K.I.5    Kitamura, N.6    Komada, M.7
  • 88
    • 77954903507 scopus 로고    scopus 로고
    • Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wg/Wnt
    • Mukai, A., Yamamoto-Hino, M., Awano, W., Watanabe, W., Komada, M. and Goto, S. (2010). Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wg/Wnt. EMBO J. 29, 2114-2125.
    • (2010) EMBO J , vol.29 , pp. 2114-2125
    • Mukai, A.1    Yamamoto-Hino, M.2    Awano, W.3    Watanabe, W.4    Komada, M.5    Goto, S.6
  • 89
    • 79958030960 scopus 로고    scopus 로고
    • The USP1/UAF1 complex promotes double-strand break repair through homologous recombination
    • Murai, J., Yang, K., Dejsuphong, D., Hirota, K., Takeda, S. and D'Andrea, A. D. (2011). The USP1/UAF1 complex promotes double-strand break repair through homologous recombination. Mol. Cell. Biol. 31, 2462-2469.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2462-2469
    • Murai, J.1    Yang, K.2    Dejsuphong, D.3    Hirota, K.4    Takeda, S.5    D'Andrea, A.D.6
  • 91
    • 38149081168 scopus 로고    scopus 로고
    • Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation
    • Nakagawa, T., Kajitani, T., Togo, S., Masuko, N., Ohdan, H., Hishikawa, Y., Koji, T., Matsuyama, T., Ikura, T., Muramatsu, M. et al. (2008). Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation. Genes Dev. 22, 37-49.
    • (2008) Genes Dev , vol.22 , pp. 37-49
    • Nakagawa, T.1    Kajitani, T.2    Togo, S.3    Masuko, N.4    Ohdan, H.5    Hishikawa, Y.6    Koji, T.7    Matsuyama, T.8    Ikura, T.9    Muramatsu, M.10
  • 92
    • 33646729226 scopus 로고    scopus 로고
    • Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes
    • Nakamura, M., Tanaka, N., Kitamura, N. and Komada, M. (2006). Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes. Genes Cells 11, 593-606.
    • (2006) Genes Cells , vol.11 , pp. 593-606
    • Nakamura, M.1    Tanaka, N.2    Kitamura, N.3    Komada, M.4
  • 93
    • 48249124967 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology by USP30, a deubiquitinating enzyme present in the mitochondrial outer membrane
    • Nakamura, N. and Hirose, S. (2008). Regulation of mitochondrial morphology by USP30, a deubiquitinating enzyme present in the mitochondrial outer membrane. Mol. Biol. Cell 19, 1903-1911.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1903-1911
    • Nakamura, N.1    Hirose, S.2
  • 98
    • 0023336183 scopus 로고
    • The yeast ubiquitin genes: a family of natural gene fusions
    • Ozkaynak, E., Finley, D., Solomon, M. J. and Varshavsky, A. (1987). The yeast ubiquitin genes: a family of natural gene fusions. EMBO J. 6, 1429-1439.
    • (1987) EMBO J , vol.6 , pp. 1429-1439
    • Ozkaynak, E.1    Finley, D.2    Solomon, M.J.3    Varshavsky, A.4
  • 99
    • 79951997444 scopus 로고    scopus 로고
    • USP47 is a deubiquitylating enzyme that regulates base excision repair by controlling steady-state levels of DNA polymerase beta
    • Parsons, J. L., Dianova, I. I., Khoronenkova, S. V., Edelmann, M. J., Kessler, B. M. and Dianov, G. L. (2011). USP47 is a deubiquitylating enzyme that regulates base excision repair by controlling steady-state levels of DNA polymerase beta. Mol. Cell 41, 609-615.
    • (2011) Mol. Cell , vol.41 , pp. 609-615
    • Parsons, J.L.1    Dianova, I.I.2    Khoronenkova, S.V.3    Edelmann, M.J.4    Kessler, B.M.5    Dianov, G.L.6
  • 100
    • 84855925244 scopus 로고    scopus 로고
    • Regulation of the activation of the Fanconi anemia pathway by the p21 cyclin-dependent kinase inhibitor
    • Rego, M. A., Harney, J. A., Mauro, M., Shen, M. and Howlett, N. G. (2011). Regulation of the activation of the Fanconi anemia pathway by the p21 cyclin-dependent kinase inhibitor. Oncogene 31, 366-375
    • (2011) Oncogene , vol.31 , pp. 366-375
    • Rego, M.A.1    Harney, J.A.2    Mauro, M.3    Shen, M.4    Howlett, N.G.5
  • 101
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu, F. E., Ventii, K. H. and Wilkinson, K. D. (2009). Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu. Rev. Biochem. 78, 363-397.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 102
    • 33646788800 scopus 로고    scopus 로고
    • The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation
    • Row, P. E., Prior, I. A., McCullough, J., Clague, M. J. and Urbe, S. (2006). The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. J. Biol. Chem. 281, 12618-12624.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12618-12624
    • Row, P.E.1    Prior, I.A.2    McCullough, J.3    Clague, M.J.4    Urbe, S.5
  • 103
    • 35648973707 scopus 로고    scopus 로고
    • The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation
    • Row, P. E., Liu, H., Hayes, S., Welchman, R., Charalabous, P., Hofmann, K., Clague, M. J., Sanderson, C. M. and Urbe, S. (2007). The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation. J. Biol. Chem. 282, 30929-30937.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30929-30937
    • Row, P.E.1    Liu, H.2    Hayes, S.3    Welchman, R.4    Charalabous, P.5    Hofmann, K.6    Clague, M.J.7    Sanderson, C.M.8    Urbe, S.9
  • 107
    • 36448936383 scopus 로고    scopus 로고
    • TGFbeta-SMAD signal transduction: molecular specificity and functional flexibility
    • Schmierer, B. and Hill, C. S. (2007). TGFbeta-SMAD signal transduction: molecular specificity and functional flexibility. Nat. Rev Mol. Cell Biol. 8, 970-982.
    • (2007) Nat. Rev Mol. Cell Biol. , vol.8 , pp. 970-982
    • Schmierer, B.1    Hill, C.S.2
  • 108
    • 62549140202 scopus 로고    scopus 로고
    • The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks
    • Shao, G., Lilli, D. R., Patterson-Fortin, J., Coleman, K. A., Morrissey, D. E. and Greenberg, R. A. (2009). The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks. Proc. Natl. Acad. Sci. USA 106, 3166-3671.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3166-3671
    • Shao, G.1    Lilli, D.R.2    Patterson-Fortin, J.3    Coleman, K.A.4    Morrissey, D.E.5    Greenberg, R.A.6
  • 109
    • 66149116039 scopus 로고    scopus 로고
    • Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2
    • Shenoy, S. K., Modi, A. S., Shukla, A. K., Xiao, K., Berthouze, M., Ahn, S., Wilkinson, K. D., Miller, W. E. and Lefkowitz, R. J. (2009). Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2. Proc. Natl. Acad. Sci. USA 106, 6650-6655.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6650-6655
    • Shenoy, S.K.1    Modi, A.S.2    Shukla, A.K.3    Xiao, K.4    Berthouze, M.5    Ahn, S.6    Wilkinson, K.D.7    Miller, W.E.8    Lefkowitz, R.J.9
  • 110
    • 33644763022 scopus 로고    scopus 로고
    • The APC tumour suppressor counteracts β-catenin activation and H3K4 methylation at Wnt target genes
    • Sierra, J., Yoshida, T., Joazeiro, C. A. and Jones, K. A. (2006). The APC tumour suppressor counteracts β-catenin activation and H3K4 methylation at Wnt target genes. Genes Dev. 20, 586-600.
    • (2006) Genes Dev , vol.20 , pp. 586-600
    • Sierra, J.1    Yoshida, T.2    Joazeiro, C.A.3    Jones, K.A.4
  • 113
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P. and Harper, J. W. (2009). Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 114
    • 58149311474 scopus 로고    scopus 로고
    • Opposing activities of the Snx3-retromer complex and ESCRT proteins mediate regulated cargo sorting at a common endosome
    • Strochlic, T. I., Schmiedekamp, B. C., Lee, J., Katzmann, D. J. and Burd, C. G. (2008). Opposing activities of the Snx3-retromer complex and ESCRT proteins mediate regulated cargo sorting at a common endosome. Mol. Biol. Cell 19, 4694-4706.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4694-4706
    • Strochlic, T.I.1    Schmiedekamp, B.C.2    Lee, J.3    Katzmann, D.J.4    Burd, C.G.5
  • 115
    • 77957005350 scopus 로고    scopus 로고
    • The various roles of ubiquitin in Wnt pathway regulation
    • Tauriello, D. V. and Maurice, M. M. (2010). The various roles of ubiquitin in Wnt pathway regulation. Cell Cycle 9, 3700-3709.
    • (2010) Cell Cycle , vol.9 , pp. 3700-3709
    • Tauriello, D.V.1    Maurice, M.M.2
  • 117
    • 27444445613 scopus 로고    scopus 로고
    • c-Cbl and Cbl-b ubiquitin ligases: substrate diversity and the negative regulation of signalling responses
    • Thien, C. B. and Langdon, W. Y. (2005). c-Cbl and Cbl-b ubiquitin ligases: substrate diversity and the negative regulation of signalling responses. Biochem. J. 391, 153-166.
    • (2005) Biochem. J. , vol.391 , pp. 153-166
    • Thien, C.B.1    Langdon, W.Y.2
  • 118
    • 80053598334 scopus 로고    scopus 로고
    • isoformspecific localization of the deubiquitinase USP33 to the Golgi apparatus
    • Thorne, C., Eccles, R. L., Coulson, J. M., Urbe, S. and Clague, M. J. (2011). isoformspecific localization of the deubiquitinase USP33 to the Golgi apparatus. Traffic 12, 1563-1574.
    • (2011) Traffic , vol.12 , pp. 1563-1574
    • Thorne, C.1    Eccles, R.L.2    Coulson, J.M.3    Urbe, S.4    Clague, M.J.5
  • 119
    • 39449084931 scopus 로고    scopus 로고
    • Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains
    • Tran, H., Hamada, F., Schwarz-Romond, T. and Bienz, M. (2008). Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains. Genes Dev. 22, 528-542.
    • (2008) Genes Dev , vol.22 , pp. 528-542
    • Tran, H.1    Hamada, F.2    Schwarz-Romond, T.3    Bienz, M.4
  • 120
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NFkappaB activation by TNFR family members
    • Trompouki, E., Hatzivassiliou, E., Tsichritzis, T., Farmer, H., Ashworth, A. and Mosialos, G. (2003). CYLD is a deubiquitinating enzyme that negatively regulates NFkappaB activation by TNFR family members. Nature 424, 793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 121
    • 74549158762 scopus 로고    scopus 로고
    • Genome-wide loss-of-function analysis of deubiquitylating enzymes for zebrafish development
    • Tse, W. K. F., Eisenhaber, B., Ho, S. H. K., Ng, Q., Eisenhaber, F. and Jiang, Y.-J. (2009). Genome-wide loss-of-function analysis of deubiquitylating enzymes for zebrafish development. BMC Genomics 10, 637.
    • (2009) BMC Genomics , vol.10 , pp. 637
    • Tse, W.K.F.1    Eisenhaber, B.2    Ho, S.H.K.3    Ng, Q.4    Eisenhaber, F.5    Jiang, Y.-J.6
  • 122
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • Ulrich, H. D. and Walden, H. (2010). Ubiquitin signalling in DNA replication and repair. Nat. Rev. Mol. Cell Biol. 11, 479-489.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 479-489
    • Ulrich, H.D.1    Walden, H.2
  • 126
    • 36749025467 scopus 로고    scopus 로고
    • Ubc13/RNF8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage
    • Wang, B. and Elledge, S. J. (2007). Ubc13/RNF8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage. Proc. Natl. Acad. Sci. USA 104, 20759-20763.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20759-20763
    • Wang, B.1    Elledge, S.J.2
  • 127
    • 33748988214 scopus 로고    scopus 로고
    • Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3
    • Wang, Q., Li, L. and Ye, Y. (2006). Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3. J. Cell Biol. 174, 963-971.
    • (2006) J. Cell Biol. , vol.174 , pp. 963-971
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 128
    • 1842509180 scopus 로고    scopus 로고
    • VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments
    • Wang, Y., Satoh, A., Warren, G. and Meyer, H. H. (2004). VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments. J. Cell Biol. 164, 973-978.
    • (2004) J. Cell Biol. , vol.164 , pp. 973-978
    • Wang, Y.1    Satoh, A.2    Warren, G.3    Meyer, H.H.4
  • 129
    • 27944498719 scopus 로고    scopus 로고
    • The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling
    • Wicks, S. J., Haros, K., Maillard, M., Song, L., Cohen, R. E., Dijke, P. T. and Chantry, A. (2005). The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling. Oncogene 24, 8080-8084.
    • (2005) Oncogene , vol.24 , pp. 8080-8084
    • Wicks, S.J.1    Haros, K.2    Maillard, M.3    Song, L.4    Cohen, R.E.5    Dijke, P.T.6    Chantry, A.7
  • 130
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • Williams, R. L. and Urbe, S. (2007). The emerging shape of the ESCRT machinery. Nat. Rev. Mol. Cell Biol. 8, 355-368.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 355-368
    • Williams, R.L.1    Urbe, S.2
  • 132
    • 69949093459 scopus 로고    scopus 로고
    • Direct activation of protein kinases by unanchored polyubiquitin chains
    • Xia, Z. P., Sun, L., Chen, X., Pineda, G., Jiang, X., Adhikari, A., Zeng, W. and Chen, Z. J. (2009). Direct activation of protein kinases by unanchored polyubiquitin chains. Nature 461, 114-119.
    • (2009) Nature , vol.461 , pp. 114-119
    • Xia, Z.P.1    Sun, L.2    Chen, X.3    Pineda, G.4    Jiang, X.5    Adhikari, A.6    Zeng, W.7    Chen, Z.J.8
  • 133
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, J., Hochstrasser, M., Finley, D. and Peng, J. (2009). Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137, 133-145.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6    Rush, J.7    Hochstrasser, M.8    Finley, D.9    Peng, J.10
  • 134
    • 33746766974 scopus 로고    scopus 로고
    • A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response
    • Zhang, D., Zaugg, K., Mak, T. W. and Elledge, S. J. (2006). A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response. Cell 126, 529-542.
    • (2006) Cell , vol.126 , pp. 529-542
    • Zhang, D.1    Zaugg, K.2    Mak, T.W.3    Elledge, S.J.4
  • 135
    • 45849133054 scopus 로고    scopus 로고
    • USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A
    • Zhang, X. Y., Pfeiffer, H. K., Thorne, A. W. and McMahon, S. B. (2008a). USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A. Cell Cycle 7, 1522-1524.
    • (2008) Cell Cycle , vol.7 , pp. 1522-1524
    • Zhang, X.Y.1    Pfeiffer, H.K.2    Thorne, A.W.3    McMahon, S.B.4
  • 136
    • 38149078715 scopus 로고    scopus 로고
    • The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression
    • Zhang, X. Y., Varthi, M., Sykes, S. M., Phillips, C., Warzecha, C., Zhu, W., Wyce, A., Thorne, A. W., Berger, S. L. and McMahon, S. B. (2008b). The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression. Mol. Cell 29, 102-111.
    • (2008) Mol. Cell , vol.29 , pp. 102-111
    • Zhang, X.Y.1    Varthi, M.2    Sykes, S.M.3    Phillips, C.4    Warzecha, C.5    Zhu, W.6    Wyce, A.7    Thorne, A.W.8    Berger, S.L.9    McMahon, S.B.10
  • 137
    • 72949089936 scopus 로고    scopus 로고
    • The ubiquitin specific protease 4 (Usp4) is a new player in the Wnt signalling pathway
    • Zhao, B., Schlesiger, C., Masucci, M. G. and Lindsten, K. (2009). The ubiquitin specific protease 4 (Usp4) is a new player in the Wnt signalling pathway. J. Cell Mol. Med. 13, 1886-1895.
    • (2009) J. Cell Mol. Med. , vol.13 , pp. 1886-1895
    • Zhao, B.1    Schlesiger, C.2    Masucci, M.G.3    Lindsten, K.4
  • 138
    • 38149068875 scopus 로고    scopus 로고
    • A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing
    • Zhao, Y., Lang, G., Ito, S., Bonnet, J., Metzger, E., Sawatsubashi, S., Suzuki, E., Le Guezennec, X., Stunnenberg, H. G., Krasnov, A. et al. (2008). A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing. Mol. Cell 29, 92-101.
    • (2008) Mol. Cell , vol.29 , pp. 92-101
    • Zhao, Y.1    Lang, G.2    Ito, S.3    Bonnet, J.4    Metzger, E.5    Sawatsubashi, S.6    Suzuki, E.7    Le Guezennec, X.8    Stunnenberg, H.G.9    Krasnov, A.10
  • 139
    • 34547730282 scopus 로고    scopus 로고
    • A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation
    • Zhu, P., Zhou, W., Wang, J., Puc, J., Ohgi, K. A., Erdjument-Bromage, H., Tempst, P., Glass, C. K. and Rosenfeld, M. G. (2007). A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation. Mol. Cell 27, 609-621.
    • (2007) Mol. Cell , vol.27 , pp. 609-621
    • Zhu, P.1    Zhou, W.2    Wang, J.3    Puc, J.4    Ohgi, K.A.5    Erdjument-Bromage, H.6    Tempst, P.7    Glass, C.K.8    Rosenfeld, M.G.9


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