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Volumn 415, Issue 3, 2008, Pages 367-375

Positional-scanning fluorigenic substrate libraries reveal unexpected specificity determinants of DUBs (deubiquitinating enzymes)

Author keywords

Combinatorial chemistry; Deubiquitinating enzyme (DUB); Fluorigenic substrate; Positional scanning substrate combinatorial library (PS SCL); Protease; Ubiquitin

Indexed keywords

COMBINATORIAL CHEMISTRY; DEUBIQUITINATING ENZYME (DUB); FLUORIGENIC SUBSTRATE; POSITIONAL-SCANNING SUBSTRATE COMBINATORIAL LIBRARY (PS-SCL); PROTEASE; UBIQUITIN;

EID: 58149159450     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20080779     Document Type: Article
Times cited : (53)

References (35)
  • 1
    • 33847705665 scopus 로고    scopus 로고
    • Role of ubiquitin- and Ubl-binding proteins in cell signaling
    • Kirkin, V. and Dikic, I. (2007) Role of ubiquitin- and Ubl-binding proteins in cell signaling. Curr. Opin. Cell. Biol. 19, 199-205
    • (2007) Curr. Opin. Cell. Biol , vol.19 , pp. 199-205
    • Kirkin, V.1    Dikic, I.2
  • 2
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher, O., Felberbaum, R. and Hochstrasser, M. (2006) Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu. Rev. Cell Dev. Biol. 22, 159-180
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 4
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart, C. M. and Eddins, M. J. (2004) Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta 1695, 55-72
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 5
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik, A. Y. and Hochstrasser, M. (2004) Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 1695, 189-207
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 6
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H. and Ciechanover, A. (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428
    • (2002) Physiol. Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 7
    • 0032794445 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast
    • 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
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2583-2594
    • Swaminathan, S.1    Amerik, A.Y.2    Hochstrasser, M.3
  • 8
    • 34247504273 scopus 로고    scopus 로고
    • Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway
    • Nikko, E. and Andre, B. (2007) Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway. Traffic 8, 566-581
    • (2007) Traffic , vol.8 , pp. 566-581
    • Nikko, E.1    Andre, B.2
  • 12
    • 0036775490 scopus 로고    scopus 로고
    • Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family
    • Borodovsky, A., Ovaa, H., Kolli, N., 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
    • (2002) Chem. Biol , vol.9 , pp. 1149-1159
    • Borodovsky, A.1    Ovaa, H.2    Kolli, N.3    Gan-Erdene, T.4    Wilkinson, K.D.5    Ploegh, H.L.6    Kessler, B.M.7
  • 13
    • 34548848530 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO)-specific proteases: Profiling the specificities and activities of human SENPs
    • Mikolajczyk, J., Drag, M., Bekes, M., Cao, J. T., Ronai, Z. and Salvesen, G. S. (2007) Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs. J. Biol. Chem. 282, 26217-26224
    • (2007) J. Biol. Chem , vol.282 , pp. 26217-26224
    • Mikolajczyk, J.1    Drag, M.2    Bekes, M.3    Cao, J.T.4    Ronai, Z.5    Salvesen, G.S.6
  • 14
    • 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. and Shi, Y. (2002) Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111, 1041-1054
    • (2002) Cell , vol.111 , pp. 1041-1054
    • 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
  • 16
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes
    • Dang, L. C., Melandri, F. D. and Stein, R. L. (1998) Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. Biochemistry 37, 1868-1879
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 17
    • 0028801196 scopus 로고
    • Kinetic studies of isopeptidase T: Modulation of peptidase activity by ubiquitin
    • Stein, R. L., Chen, Z. and Melandri, F. (1995) Kinetic studies of isopeptidase T: modulation of peptidase activity by ubiquitin. Biochemistry 34, 12616-12623
    • (1995) Biochemistry , vol.34 , pp. 12616-12623
    • Stein, R.L.1    Chen, Z.2    Melandri, F.3
  • 18
    • 35348931646 scopus 로고    scopus 로고
    • Mechanisms, biology and inhibitors of deubiquitinating enzymes
    • Love, K. R., Catic, A., Schlieker, C. and Ploegh, H. L. (2007) Mechanisms, biology and inhibitors of deubiquitinating enzymes. Nat. Chem. Biol. 3, 697-705
    • (2007) Nat. Chem. Biol , vol.3 , pp. 697-705
    • Love, K.R.1    Catic, A.2    Schlieker, C.3    Ploegh, H.L.4
  • 19
    • 20344394159 scopus 로고    scopus 로고
    • Deubiquitinating enzyme purification, assay inhibitors, and characterization
    • Russell, N. S. and Wilkinson, K. D. (2005) Deubiquitinating enzyme purification, assay inhibitors, and characterization. Methods Mol. Biol. 301, 207-219
    • (2005) Methods Mol. Biol , vol.301 , pp. 207-219
    • Russell, N.S.1    Wilkinson, K.D.2
  • 20
    • 34249790592 scopus 로고    scopus 로고
    • Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63
    • Chen, Z., Wang, Y., Ratia, K., Mesecar, A. D., Wilkinson, K. D. and Baker, S. C. (2007) Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63. J. Virol. 81, 6007-6018
    • (2007) J. Virol , vol.81 , pp. 6007-6018
    • Chen, Z.1    Wang, Y.2    Ratia, K.3    Mesecar, A.D.4    Wilkinson, K.D.5    Baker, S.C.6
  • 21
    • 38749124386 scopus 로고    scopus 로고
    • Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family
    • Drag, M., Mikolajczyk, J., Krishnakumar, I. M., Huang, Z. and Salvesen, G. S. (2008) Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family. Biochem. J. 409, 461-469
    • (2008) Biochem. J , vol.409 , pp. 461-469
    • Drag, M.1    Mikolajczyk, J.2    Krishnakumar, I.M.3    Huang, Z.4    Salvesen, G.S.5
  • 22
    • 0030091649 scopus 로고    scopus 로고
    • α-protected aminoacyl 7-amino-4-methyl-coumarin amide by phosphorus oxychloride and preparation of specific fluorogenic substrates for papain
    • α-protected aminoacyl 7-amino-4-methyl-coumarin amide by phosphorus oxychloride and preparation of specific fluorogenic substrates for papain. Pept. Res. 9, 92-96
    • (1996) Pept. Res , vol.9 , pp. 92-96
    • Alves, L.C.1    Almeida, P.C.2    Franzoni, L.3    Juliano, L.4    Juliano, M.A.5
  • 23
    • 0033515621 scopus 로고    scopus 로고
    • An alkanesulfonamide "safety-catch" linker for solid-phase synthesis
    • Backes, B. J. and Ellman, J. A. (1999) An alkanesulfonamide "safety-catch" linker for solid-phase synthesis. J. Org. Chem. 64, 2322-2330
    • (1999) J. Org. Chem , vol.64 , pp. 2322-2330
    • Backes, B.J.1    Ellman, J.A.2
  • 25
    • 29744455503 scopus 로고    scopus 로고
    • The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity
    • Barretto, N., Jukneliene, D., Ratia, K., Chen, Z., Mesecar, A. D. and Baker, S. C. (2005) The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity. J. Virol. 79, 15189-15198
    • (2005) J. Virol , vol.79 , pp. 15189-15198
    • Barretto, N.1    Jukneliene, D.2    Ratia, K.3    Chen, Z.4    Mesecar, A.D.5    Baker, S.C.6
  • 26
    • 0037039894 scopus 로고    scopus 로고
    • Expedient solid-phase synthesis of fluorogenic protease substrates using the 7-amino-4-carbamoylmethylcoumarin (ACC) fluorophore
    • Maly, D. J., Leonetti, F., Backes, B. J., Dauber, D. S., Harris, J. L., Craik, C. S. and Ellman, J. A. (2002) Expedient solid-phase synthesis of fluorogenic protease substrates using the 7-amino-4-carbamoylmethylcoumarin (ACC) fluorophore. J. Org. Chem. 67, 910-915
    • (2002) J. Org. Chem , vol.67 , pp. 910-915
    • Maly, D.J.1    Leonetti, F.2    Backes, B.J.3    Dauber, D.S.4    Harris, J.L.5    Craik, C.S.6    Ellman, J.A.7
  • 27
    • 33744961634 scopus 로고    scopus 로고
    • Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities
    • Choe, Y., Leonetti, F., Greenbaum, D. C., Lecaille, F., Bogyo, M., Bromme, D., Ellman, J. A. and Craik, C. S. (2006) Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J. Biol. Chem. 281, 12824-12832
    • (2006) J. Biol. Chem , vol.281 , pp. 12824-12832
    • Choe, Y.1    Leonetti, F.2    Greenbaum, D.C.3    Lecaille, F.4    Bogyo, M.5    Bromme, D.6    Ellman, J.A.7    Craik, C.S.8
  • 28
    • 0034608931 scopus 로고    scopus 로고
    • Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries
    • Harris, J. L., Backes, B. J., Leonetti, F., Mahrus, S., Ellman, J. A. and Craik, C. S. (2000) Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc. Natl. Acad. Sci. U.S.A. 97, 7754-7759
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 7754-7759
    • Harris, J.L.1    Backes, B.J.2    Leonetti, F.3    Mahrus, S.4    Ellman, J.A.5    Craik, C.S.6
  • 29
    • 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
  • 30
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å 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 1.8 Å 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
  • 31
    • 33646066025 scopus 로고    scopus 로고
    • The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin
    • Reyes-Turcu, F. E., Horton, J. R., Mullally, J. E., Heroux, A., Cheng, X. and Wilkinson, K. D. (2006) The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin. Cell 124, 1197-1208
    • (2006) Cell , vol.124 , pp. 1197-1208
    • Reyes-Turcu, F.E.1    Horton, J.R.2    Mullally, J.E.3    Heroux, A.4    Cheng, X.5    Wilkinson, K.D.6
  • 32
    • 33751408436 scopus 로고    scopus 로고
    • Interactions between macromolecules and ions: The Hofmeister series
    • Zhang, Y. and Cremer, P. S. (2006) Interactions between macromolecules and ions: the Hofmeister series. Curr. Opin. Chem. Biol. 10, 658-663
    • (2006) Curr. Opin. Chem. Biol , vol.10 , pp. 658-663
    • Zhang, Y.1    Cremer, P.S.2
  • 33
    • 34247130575 scopus 로고    scopus 로고
    • Human coronavirus 229E papain-like proteases have overlapping specificities but distinct functions in viral replication
    • Ziebuhr, J., Schelle, B., Karl, N., Minskaia, E., Bayer, S., Siddell, S. G., Gorbalenya, A. E. and Thiel, V. (2007) Human coronavirus 229E papain-like proteases have overlapping specificities but distinct functions in viral replication. J. Virol. 81, 3922-3932
    • (2007) J. Virol , vol.81 , pp. 3922-3932
    • Ziebuhr, J.1    Schelle, B.2    Karl, N.3    Minskaia, E.4    Bayer, S.5    Siddell, S.G.6    Gorbalenya, A.E.7    Thiel, V.8


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