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Volumn 466, Issue 3, 2015, Pages 489-498

Ubiquitin C-terminal hydrolases cleave isopeptide- and peptide-linked ubiquitin from structured proteins but do not edit ubiquitin homopolymers

Author keywords

BAP1; SUMO; Ube2W; Ubiquitin; UCH L1; UCH L3; UCH L5

Indexed keywords

LYSINE; PEPTIDE; POLYMER; PROTEIN UBE2W; SUMO 2 PROTEIN; UBIQUITIN; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; SUMO PROTEIN; SUMO2 PROTEIN, HUMAN;

EID: 84934949377     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141349     Document Type: Article
Times cited : (39)

References (48)
  • 2
    • 84898734084 scopus 로고    scopus 로고
    • Lysine-targeting specificity in ubiquitin and ubiquitin-like modification pathways
    • Mattiroli, F. and Sixma, T. K. (2014) Lysine-targeting specificity in ubiquitin and ubiquitin-like modification pathways. Nat. Struct. Mol. Biol. 21, 308-316
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 308-316
    • Mattiroli, F.1    Sixma, T.K.2
  • 4
    • 0032531925 scopus 로고    scopus 로고
    • A novel site for ubiquitination: The N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein
    • Breitschopf, K., Bengal, E., Ziv, T., Admon, A. and Ciechanover, A. (1998) A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J. 17, 5964-5973
    • (1998) EMBO J. , vol.17 , pp. 5964-5973
    • Breitschopf, K.1    Bengal, E.2    Ziv, T.3    Admon, A.4    Ciechanover, A.5
  • 5
    • 0141987892 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation
    • Bloom, J., Amador, V., Bartolini, F., De Martino, G. and Pagano, M. (2003) Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation. Cell 115, 71-82
    • (2003) Cell , vol.115 , pp. 71-82
    • Bloom, J.1    Amador, V.2    Bartolini, F.3    De Martino, G.4    Pagano, M.5
  • 6
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: More protein substrates join in
    • Ciechanover, A. and Ben-Saadon, R. (2004) N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol. 14, 103-106
    • (2004) Trends Cell Biol. , vol.14 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 7
    • 84879008640 scopus 로고    scopus 로고
    • Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini
    • Tatham, M. H., Plechanovova, A., Jaffray, E. G., Salmen, H. and Hay, R. T. (2013) Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini. Biochem. J. 453, 137-145
    • (2013) Biochem. J. , vol.453 , pp. 137-145
    • Tatham, M.H.1    Plechanovova, A.2    Jaffray, E.G.3    Salmen, H.4    Hay, R.T.5
  • 11
    • 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
  • 14
  • 16
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8A° resolution
    • Johnston, S. C., Larsen, C. N., Cook, W. J., Wilkinson, K. D. and Hill, C. P. (1997) Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8A° resolution. EMBO J. 16, 3787-3796
    • (1997) EMBO J. , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 17
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • Johnston, S. C., Riddle, S. M., Cohen, R. E. and Hill, C. P. (1999) Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18, 3877-3887
    • (1999) EMBO J. , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 19
    • 12544253837 scopus 로고    scopus 로고
    • Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate
    • Misaghi, S., Galardy, P. J., Meester, W. J., Ovaa, H., Ploegh, H. L. and Gaudet, R. (2005) Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate. J. Biol. Chem. 280, 1512-1520
    • (2005) J. Biol. Chem. , vol.280 , pp. 1512-1520
    • Misaghi, S.1    Galardy, P.J.2    Meester, W.J.3    Ovaa, H.4    Ploegh, H.L.5    Gaudet, R.6
  • 21
    • 84890190983 scopus 로고    scopus 로고
    • Regulation of proteolysis by human deubiquitinating enzymes
    • Eletr, Z. M. and Wilkinson, K. D. (2014) Regulation of proteolysis by human deubiquitinating enzymes. Biochim. Biophys. Acta 1843, 114-128
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 114-128
    • Eletr, Z.M.1    Wilkinson, K.D.2
  • 22
    • 0020555640 scopus 로고
    • An enzyme with ubiquitin carboxy-terminal esterase activity from reticulocytes
    • Rose, I. A. and Warms, J. V. (1983) An enzyme with ubiquitin carboxy-terminal esterase activity from reticulocytes. Biochemistry 22, 4234-4237
    • (1983) Biochemistry , vol.22 , pp. 4234-4237
    • Rose, I.A.1    Warms, J.V.2
  • 23
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
    • Komander, D., Reyes-Turcu, F., Licchesi, J. D., Odenwaelder, P., Wilkinson, K. D. and Barford, D. (2009) Molecular discrimination of structurally equivalent Lys 63-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
  • 24
    • 0021929906 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides
    • Pickart, C. M. and Rose, I. A. (1985) Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. J. Biol. Chem. 260, 7903-7910 PubMed
    • (1985) J. Biol. Chem. , vol.260 , pp. 7903-7910
    • Pickart, C.M.1    Rose, I.A.2
  • 26
    • 0032502276 scopus 로고    scopus 로고
    • Substrate specificity of deubiquitinating enzymes: Ubiquitin C-terminal hydrolases
    • Larsen, C. N., Krantz, B. A. and Wilkinson, K. D. (1998) Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. Biochemistry 37, 3358-3368
    • (1998) Biochemistry , vol.37 , pp. 3358-3368
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 29
    • 46449134021 scopus 로고    scopus 로고
    • ElaD, a deubiquitinating protease expressed by E. Coli
    • Catic, A., Misaghi, S., Korbel, G. A. and Ploegh, H. L. (2007) ElaD, a deubiquitinating protease expressed by E. coli. PLoS One 2, e381
    • (2007) PLoS One , vol.2 , pp. e381
    • Catic, A.1    Misaghi, S.2    Korbel, G.A.3    Ploegh, H.L.4
  • 30
    • 77956903406 scopus 로고    scopus 로고
    • Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase
    • Virdee, S., Ye, Y., Nguyen, D. P., Komander, D. and Chin, J. W. (2010) Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase. Nat. Chem. Biol. 6, 750-757
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 750-757
    • Virdee, S.1    Ye, Y.2    Nguyen, D.P.3    Komander, D.4    Chin, J.W.5
  • 34
    • 80051799492 scopus 로고    scopus 로고
    • Mutant ubiquitin (UBB+1) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3)
    • Dennissen, F. J., Kholod, N., Hermes, D. J., Kemmerling, N., Steinbusch, H. W., Dantuma, N. P. and Van Leeuwen, F. W. (2011) Mutant ubiquitin (UBB+1) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3). FEBS Lett. 585, 2568-2574
    • (2011) FEBS Lett. , vol.585 , pp. 2568-2574
    • Dennissen, F.J.1    Kholod, N.2    Hermes, D.J.3    Kemmerling, N.4    Steinbusch, H.W.5    Dantuma, N.P.6    Van Leeuwen, F.W.7
  • 35
    • 84861574737 scopus 로고    scopus 로고
    • The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE (OMe)-FMK)
    • Davies, C. W., Chaney, J., Korbel, G., Ringe, D., Petsko, G. A., Ploegh, H. and Das, C. (2012) The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE (OMe)-FMK). Bioorg. Med. Chem. Lett. 22, 3900-3904
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 3900-3904
    • Davies, C.W.1    Chaney, J.2    Korbel, G.3    Ringe, D.4    Petsko, G.A.5    Ploegh, H.6    Das, C.7
  • 36
    • 63649131003 scopus 로고    scopus 로고
    • Substrate filtering by the active site crossover loop in UCHL3 revealed by sortagging and gain-of-function mutations
    • Popp, M. W., Artavanis-Tsakonas, K. and Ploegh, H. L. (2009) Substrate filtering by the active site crossover loop in UCHL3 revealed by sortagging and gain-of-function mutations. J. Biol. Chem. 284, 3593-3602
    • (2009) J. Biol. Chem. , vol.284 , pp. 3593-3602
    • Popp, M.W.1    Artavanis-Tsakonas, K.2    Ploegh, H.L.3
  • 37
    • 61449129071 scopus 로고    scopus 로고
    • Ubiquitin dimers control the hydrolase activity of UCH-L3
    • Setsuie, R., Sakurai, M., Sakaguchi, Y. and Wada, K. (2009) Ubiquitin dimers control the hydrolase activity of UCH-L3. Neurochem. Int. 54, 314-321
    • (2009) Neurochem. Int. , vol.54 , pp. 314-321
    • Setsuie, R.1    Sakurai, M.2    Sakaguchi, Y.3    Wada, K.4
  • 38
    • 4143083663 scopus 로고    scopus 로고
    • A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
    • Reverter, D. and Lima, C. D. (2004) A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. Structure 12, 1519-1531
    • (2004) Structure , vol.12 , pp. 1519-1531
    • Reverter, D.1    Lima, C.D.2
  • 39
    • 33845370047 scopus 로고    scopus 로고
    • Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
    • Reverter, D. and Lima, C. D. (2006) Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nat. Struct. Mol. Biol. 13, 1060-1068
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1060-1068
    • Reverter, D.1    Lima, C.D.2
  • 40
    • 33746038148 scopus 로고    scopus 로고
    • The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing
    • Shen, L. N., Dong, C., Liu, H., Naismith, J. H. and Hay, R. T. (2006) The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem. J. 397, 279-288
    • (2006) Biochem. J. , vol.397 , pp. 279-288
    • Shen, L.N.1    Dong, C.2    Liu, H.3    Naismith, J.H.4    Hay, R.T.5
  • 42
    • 84923332311 scopus 로고    scopus 로고
    • Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding
    • Chen, C. H., Namanja, A. T. and Chen, Y. (2014) Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding. Nat. Commun. 5, 4968
    • (2014) Nat. Commun. , vol.5 , pp. 4968
    • Chen, C.H.1    Namanja, A.T.2    Chen, Y.3
  • 43
    • 84055178186 scopus 로고    scopus 로고
    • Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains
    • Zhou, Z. R., Zhang, Y. H., Liu, S., Song, A. X. and Hu, H. Y. (2012) Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains. Biochem. J. 441, 143-149
    • (2012) Biochem. J. , vol.441 , pp. 143-149
    • Zhou, Z.R.1    Zhang, Y.H.2    Liu, S.3    Song, A.X.4    Hu, H.Y.5
  • 45
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E. S., Ma, P. C., Ota, I. M. and Varshavsky, A. (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 46
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8A° resolution
    • Vijay-Kumar, S., Bugg, C. E. and Cook, W. J. (1987) Structure of ubiquitin refined at 1.8A° resolution. J. Mol. Biol. 194, 531-544
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 47
    • 7044269671 scopus 로고    scopus 로고
    • Crystal structures of the human SUMO-2 protein at 1.6A° and 1.2A° resolution: Implication on the functional differences of SUMO proteins
    • Huang, W. C., Ko, T. P., Li, S. S. and Wang, A. H. (2004) Crystal structures of the human SUMO-2 protein at 1.6A° and 1.2A° resolution: implication on the functional differences of SUMO proteins. Eur. J. Biochem. 271, 4114-4122
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4114-4122
    • Huang, W.C.1    Ko, T.P.2    Li, S.S.3    Wang, A.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.