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Volumn 23, Issue 6, 2013, Pages 806-811

Regulation of deubiquitinase proteolytic activity

Author keywords

[No Author keywords available]

Indexed keywords

DEUBIQUITINASE; PEPTIDES AND PROTEINS; POLYUBIQUITIN; PROTEIN SGF11; PROTEIN SGF73; PROTEIN SUS1; PROTEINASE; REACTIVE OXYGEN METABOLITE; UBIQUITIN; UBIQUITIN ALDEHYDE; UNCLASSIFIED DRUG;

EID: 84888437178     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2013.07.012     Document Type: Review
Times cited : (24)

References (42)
  • 1
    • 34347265174 scopus 로고    scopus 로고
    • Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins
    • Dye B.T., Schulman B.A. Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins. Annu Rev Biophys Biomol Struct 2007, 36:131-150.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 131-150
    • Dye, B.T.1    Schulman, B.A.2
  • 2
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu F.E., Ventii K.H., Wilkinson K.D. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem 2009, 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
  • 4
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik A.Y., Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim Biophys Acta 2004, 1695:189-207.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 6
    • 79955941973 scopus 로고    scopus 로고
    • PTMs in conversation: activity and function of deubiquitinating enzymes regulated via post-translational modifications
    • Kessler B.M., Edelmann M.J. PTMs in conversation: activity and function of deubiquitinating enzymes regulated via post-translational modifications. Cell Biochem Biophys 2011, 60:21-38.
    • (2011) Cell Biochem Biophys , vol.60 , pp. 21-38
    • Kessler, B.M.1    Edelmann, M.J.2
  • 7
    • 18144368948 scopus 로고    scopus 로고
    • Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation
    • Reiley W., Zhang M., Wu X., Granger E., Sun S.C. Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation. Mol Cell Biol 2005, 25:3886-3895.
    • (2005) Mol Cell Biol , vol.25 , pp. 3886-3895
    • Reiley, W.1    Zhang, M.2    Wu, X.3    Granger, E.4    Sun, S.C.5
  • 8
    • 65649114699 scopus 로고    scopus 로고
    • Phosphorylation of the tumor suppressor CYLD by the breast cancer oncogene IKKepsilon promotes cell transformation
    • Hutti J.E., Shen R.R., Abbott D.W., Zhou A.Y., Sprott K.M., Asara J.M., Hahn W.C., Cantley L.C. Phosphorylation of the tumor suppressor CYLD by the breast cancer oncogene IKKepsilon promotes cell transformation. Mol Cell 2009, 34:461-472.
    • (2009) Mol Cell , vol.34 , pp. 461-472
    • Hutti, J.E.1    Shen, R.R.2    Abbott, D.W.3    Zhou, A.Y.4    Sprott, K.M.5    Asara, J.M.6    Hahn, W.C.7    Cantley, L.C.8
  • 10
    • 78649811312 scopus 로고    scopus 로고
    • Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117
    • Todi S.V., Scaglione K.M., Blount J.R., Basrur V., Conlon K.P., Pastore A., Elenitoba-Johnson K., Paulson H.L. Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117. J Biol Chem 2010, 285:39303-39313.
    • (2010) J Biol Chem , vol.285 , pp. 39303-39313
    • Todi, S.V.1    Scaglione, K.M.2    Blount, J.R.3    Basrur, V.4    Conlon, K.P.5    Pastore, A.6    Elenitoba-Johnson, K.7    Paulson, H.L.8
  • 11
    • 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., D'Andrea A.D. A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway. Mol Cell 2007, 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
  • 12
    • 84859410891 scopus 로고    scopus 로고
    • A noncanonical cysteine protease USP1 is activated through active site modulation by USP1-associated factor 1
    • Villamil M.A., Chen J., Liang Q., Zhuang Z. A noncanonical cysteine protease USP1 is activated through active site modulation by USP1-associated factor 1. Biochemistry 2012, 51:2829-2839.
    • (2012) Biochemistry , vol.51 , pp. 2829-2839
    • Villamil, M.A.1    Chen, J.2    Liang, Q.3    Zhuang, Z.4
  • 13
    • 84869068767 scopus 로고    scopus 로고
    • Serine phosphorylation is critical for the activation of ubiquitin-specific protease 1 and its interaction with WD40-repeat protein UAF1
    • Villamil M.A., Liang Q., Chen J., Choi Y.S., Hou S., Lee K.H., Zhuang Z. Serine phosphorylation is critical for the activation of ubiquitin-specific protease 1 and its interaction with WD40-repeat protein UAF1. Biochemistry 2012, 51:9112-9123.
    • (2012) Biochemistry , vol.51 , pp. 9112-9123
    • Villamil, M.A.1    Liang, Q.2    Chen, J.3    Choi, Y.S.4    Hou, S.5    Lee, K.H.6    Zhuang, Z.7
  • 16
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa M.E., Bennett E.J., Gygi S.P., Harper J.W. Defining the human deubiquitinating enzyme interaction landscape. Cell 2009, 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
  • 18
    • 52049112825 scopus 로고    scopus 로고
    • Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex
    • Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., et al. Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex. Mol Cell 2008, 31:909-917.
    • (2008) Mol Cell , vol.31 , pp. 909-917
    • Yao, T.1    Song, L.2    Jin, J.3    Cai, Y.4    Takahashi, H.5    Swanson, S.K.6    Washburn, M.P.7    Florens, L.8    Conaway, R.C.9    Cohen, R.E.10
  • 19
    • 64149129169 scopus 로고    scopus 로고
    • UAF1 is a subunit of multiple deubiquitinating enzyme complexes
    • Cohn M.A., Kee Y., Haas W., Gygi S.P., D'Andrea A.D. UAF1 is a subunit of multiple deubiquitinating enzyme complexes. J Biol Chem 2009, 284:5343-5351.
    • (2009) J Biol Chem , vol.284 , pp. 5343-5351
    • Cohn, M.A.1    Kee, Y.2    Haas, W.3    Gygi, S.P.4    D'Andrea, A.D.5
  • 20
    • 77951247308 scopus 로고    scopus 로고
    • WDR20 regulates activity of the USP12 x UAF1 deubiquitinating enzyme complex
    • Kee Y., Yang K., Cohn M.A., Haas W., Gygi S.P., D'Andrea A.D. WDR20 regulates activity of the USP12 x UAF1 deubiquitinating enzyme complex. J Biol Chem 2010, 285:11252-11257.
    • (2010) J Biol Chem , vol.285 , pp. 11252-11257
    • Kee, Y.1    Yang, K.2    Cohn, M.A.3    Haas, W.4    Gygi, S.P.5    D'Andrea, A.D.6
  • 24
    • 73449097872 scopus 로고    scopus 로고
    • EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication
    • Sarkari F., Sanchez-Alcaraz T., Wang S., Holowaty M.N., Sheng Y., Frappier L. EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication. PLoS Pathog 2009, 5:e1000624.
    • (2009) PLoS Pathog , vol.5
    • Sarkari, F.1    Sanchez-Alcaraz, T.2    Wang, S.3    Holowaty, M.N.4    Sheng, Y.5    Frappier, L.6
  • 25
    • 80053594090 scopus 로고    scopus 로고
    • Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase
    • Faesen A.C., Dirac A.M., Shanmugham A., Ovaa H., Perrakis A., Sixma T.K. Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase. Mol Cell 2011, 44:147-159.
    • (2011) Mol Cell , vol.44 , pp. 147-159
    • Faesen, A.C.1    Dirac, A.M.2    Shanmugham, A.3    Ovaa, H.4    Perrakis, A.5    Sixma, T.K.6
  • 26
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu M., Li P., Li M., Li W., Yao T., Wu J.W., Gu W., Cohen R.E., Shi Y. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 2002, 111:1041-1154.
    • (2002) Cell , vol.111 , pp. 1041-1154
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 27
    • 84858329099 scopus 로고    scopus 로고
    • ATAC-king the complexity of SAGA during evolution
    • Spedale G., Timmers H.T., Pijnappel W.W. ATAC-king the complexity of SAGA during evolution. Genes Dev 2012, 25:527-541.
    • (2012) Genes Dev , vol.25 , pp. 527-541
    • Spedale, G.1    Timmers, H.T.2    Pijnappel, W.W.3
  • 29
    • 12844277462 scopus 로고    scopus 로고
    • The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex
    • Lee K.K., Florens L., Swanson S.K., Washburn M.P., Workman J.L. The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex. Mol Cell Biol 2005, 25:1173-1182.
    • (2005) Mol Cell Biol , vol.25 , pp. 1173-1182
    • Lee, K.K.1    Florens, L.2    Swanson, S.K.3    Washburn, M.P.4    Workman, J.L.5
  • 30
    • 34147111657 scopus 로고    scopus 로고
    • Multi-tasking on chromatin with the SAGA coactivator complexes
    • Daniel J.A., Grant P.A. Multi-tasking on chromatin with the SAGA coactivator complexes. Mutat Res 2007, 618.
    • (2007) Mutat Res , pp. 618
    • Daniel, J.A.1    Grant, P.A.2
  • 31
    • 44649179312 scopus 로고    scopus 로고
    • Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export
    • Köhler A., Schneider M., Cabal G.G., Nehrbass U., Hurt E. Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export. Nat Cell Biol 2008, 10:707-715.
    • (2008) Nat Cell Biol , vol.10 , pp. 707-715
    • Köhler, A.1    Schneider, M.2    Cabal, G.G.3    Nehrbass, U.4    Hurt, E.5
  • 32
    • 77952519938 scopus 로고    scopus 로고
    • Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module
    • Köhler A., Zimmerman E., Schneider M., Hurt E., Zheng N. Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module. Cell 2010, 141:606-617.
    • (2010) Cell , vol.141 , pp. 606-617
    • Köhler, A.1    Zimmerman, E.2    Schneider, M.3    Hurt, E.4    Zheng, N.5
  • 33
    • 77953060092 scopus 로고    scopus 로고
    • Structural insights into the assembly and function of the SAGA deubiquitinating module
    • Samara N.L., Datta A.B., Berndsen C.E., Zhang X., Yao T., Cohen R.E., Wolberger C. Structural insights into the assembly and function of the SAGA deubiquitinating module. Science 2010, 328:1025-1029.
    • (2010) Science , vol.328 , pp. 1025-1029
    • Samara, N.L.1    Datta, A.B.2    Berndsen, C.E.3    Zhang, X.4    Yao, T.5    Cohen, R.E.6    Wolberger, C.7
  • 34
    • 84877295098 scopus 로고    scopus 로고
    • Oxidation controls the DUB step
    • Clague M.J. Oxidation controls the DUB step. Nature 2013, 497:49-50.
    • (2013) Nature , vol.497 , pp. 49-50
    • Clague, M.J.1
  • 35
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • Ray P.D., Huang B.W., Tsuji Y. Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell Signal 2012, 24:981-990.
    • (2012) Cell Signal , vol.24 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 36
    • 79959340042 scopus 로고    scopus 로고
    • Protein sulfenic acid formation: from cellular damage to redox regulation
    • Roos G., Messens J. Protein sulfenic acid formation: from cellular damage to redox regulation. Free Radic Biol Med 2011, 51:314-326.
    • (2011) Free Radic Biol Med , vol.51 , pp. 314-326
    • Roos, G.1    Messens, J.2
  • 37
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 2002, 419:135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 41
    • 84875912087 scopus 로고    scopus 로고
    • Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells
    • Lee J.G., Baek K., Soetandyo N., Ye Y. Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells. Nat Commun 2013, 4:1568.
    • (2013) Nat Commun , vol.4 , pp. 1568
    • Lee, J.G.1    Baek, K.2    Soetandyo, N.3    Ye, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.