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Volumn 20, Issue 4, 2013, Pages 604-613

An electrophoretic mobility shift assay identifies a mechanistically unique inhibitor of protein sumoylation

Author keywords

[No Author keywords available]

Indexed keywords

DNA TOPOISOMERASE; FLAVONOID; SUMO 1 PROTEIN; SUMO PROTEIN;

EID: 84876486754     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2013.04.001     Document Type: Article
Times cited : (75)

References (53)
  • 2
    • 11144324990 scopus 로고    scopus 로고
    • Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the response to DNA damage
    • E.A. Andrews, J. Palecek, J. Sergeant, E. Taylor, A.R. Lehmann, and F.Z. Watts Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the response to DNA damage Mol. Cell. Biol. 25 2005 185 196
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 185-196
    • Andrews, E.A.1    Palecek, J.2    Sergeant, J.3    Taylor, E.4    Lehmann, A.R.5    Watts, F.Z.6
  • 3
    • 78650824534 scopus 로고    scopus 로고
    • Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets
    • L. Bedford, J. Lowe, L.R. Dick, R.J. Mayer, and J.E. Brownell Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets Nat. Rev. Drug Discov. 10 2011 29 46
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 29-46
    • Bedford, L.1    Lowe, J.2    Dick, L.R.3    Mayer, R.J.4    Brownell, J.E.5
  • 5
    • 70350117089 scopus 로고    scopus 로고
    • A toolbox approach to high-throughput TR-FRET-based SUMOylation and DeSUMOylation assays
    • C.B. Carlson, R.A. Horton, and K.W. Vogel A toolbox approach to high-throughput TR-FRET-based SUMOylation and DeSUMOylation assays Assay Drug Dev. Technol. 7 2009 348 355
    • (2009) Assay Drug Dev. Technol. , vol.7 , pp. 348-355
    • Carlson, C.B.1    Horton, R.A.2    Vogel, K.W.3
  • 7
    • 4544386818 scopus 로고    scopus 로고
    • In vitro modification of human centromere protein CENP-C fragments by small ubiquitin-like modifier (SUMO) protein: Definitive identification of the modification sites by tandem mass spectrometry analysis of the isopeptides
    • T.L. Chung, H.H. Hsiao, Y.Y. Yeh, H.L. Shia, Y.L. Chen, P.H. Liang, A.H. Wang, K.H. Khoo, and S. Shoei-Lung Li In vitro modification of human centromere protein CENP-C fragments by small ubiquitin-like modifier (SUMO) protein: definitive identification of the modification sites by tandem mass spectrometry analysis of the isopeptides J. Biol. Chem. 279 2004 39653 39662
    • (2004) J. Biol. Chem. , vol.279 , pp. 39653-39662
    • Chung, T.L.1    Hsiao, H.H.2    Yeh, Y.Y.3    Shia, H.L.4    Chen, Y.L.5    Liang, P.H.6    Wang, A.H.7    Khoo, K.H.8    Shoei-Lung Li, S.9
  • 8
    • 79251473377 scopus 로고    scopus 로고
    • Will the ubiquitin system furnish as many drug targets as protein kinases?
    • P. Cohen, and M. Tcherpakov Will the ubiquitin system furnish as many drug targets as protein kinases? Cell 143 2010 686 693
    • (2010) Cell , vol.143 , pp. 686-693
    • Cohen, P.1    Tcherpakov, M.2
  • 11
    • 0035422206 scopus 로고    scopus 로고
    • Ubiquitin/26S proteasome-mediated degradation of topoisomerase i as a resistance mechanism to camptothecin in tumor cells
    • S.D. Desai, T.K. Li, A. Rodriguez-Bauman, E.H. Rubin, and L.F. Liu Ubiquitin/26S proteasome-mediated degradation of topoisomerase I as a resistance mechanism to camptothecin in tumor cells Cancer Res. 61 2001 5926 5932
    • (2001) Cancer Res. , vol.61 , pp. 5926-5932
    • Desai, S.D.1    Li, T.K.2    Rodriguez-Bauman, A.3    Rubin, E.H.4    Liu, L.F.5
  • 12
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • J.M. Desterro, M.S. Rodriguez, and R.T. Hay SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation Mol. Cell 2 1998 233 239
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 14
    • 61749102005 scopus 로고    scopus 로고
    • Targeting the SUMO E2 conjugating enzyme Ubc9 interaction for anti-cancer drug design
    • X. Duan, J.O. Trent, and H. Ye Targeting the SUMO E2 conjugating enzyme Ubc9 interaction for anti-cancer drug design Anticancer. Agents Med. Chem. 9 2009 51 54
    • (2009) Anticancer. Agents Med. Chem. , vol.9 , pp. 51-54
    • Duan, X.1    Trent, J.O.2    Ye, H.3
  • 15
    • 77952743473 scopus 로고    scopus 로고
    • An electrophoretic mobility shift assay for the identification and kinetic analysis of acetyl transferase inhibitors
    • C. Fanslau, D. Pedicord, S. Nagulapalli, H. Gray, S. Pang, L. Jayaraman, J. Lippy, and Y. Blat An electrophoretic mobility shift assay for the identification and kinetic analysis of acetyl transferase inhibitors Anal. Biochem. 402 2010 65 68
    • (2010) Anal. Biochem. , vol.402 , pp. 65-68
    • Fanslau, C.1    Pedicord, D.2    Nagulapalli, S.3    Gray, H.4    Pang, S.5    Jayaraman, L.6    Lippy, J.7    Blat, Y.8
  • 18
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • J.R. Gareau, and C.D. Lima The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition Nat. Rev. Mol. Cell Biol. 11 2010 861 871
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 19
    • 78650109515 scopus 로고    scopus 로고
    • Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies
    • M.C. Geoffroy, E.G. Jaffray, K.J. Walker, and R.T. Hay Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies Mol. Biol. Cell 21 2010 4227 4239
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4227-4239
    • Geoffroy, M.C.1    Jaffray, E.G.2    Walker, K.J.3    Hay, R.T.4
  • 22
    • 0029555190 scopus 로고
    • Antimutagenic activities of 24 synthetic flavones with the Salmonella microsomal assay
    • M. Laget, M. DeMeo, J.C. Wallet, E.M. Gaydou, H. Guiraud, and G. Dumenil Antimutagenic activities of 24 synthetic flavones with the Salmonella microsomal assay Arch. Pharm. Res. 18 1995 415 422
    • (1995) Arch. Pharm. Res. , vol.18 , pp. 415-422
    • Laget, M.1    Demeo, M.2    Wallet, J.C.3    Gaydou, E.M.4    Guiraud, H.5    Dumenil, G.6
  • 23
    • 0041317053 scopus 로고    scopus 로고
    • Total synthesis of the ubiquitin-activating enzyme inhibitor (+)-panepophenanthrin
    • X. Lei, R.P. Johnson, and J.A. Porco Jr. Total synthesis of the ubiquitin-activating enzyme inhibitor (+)-panepophenanthrin Angew. Chem. Int. Ed. Engl. 42 2003 3913 3917
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , pp. 3913-3917
    • Lei, X.1    Johnson, R.P.2    Porco Jr., J.A.3
  • 24
    • 82755176332 scopus 로고    scopus 로고
    • Nuclear translocation of cellular retinoic acid-binding protein II is regulated by retinoic acid-controlled SUMOylation
    • A. Majumdar, A.D. Petrescu, Y. Xiong, and N. Noy Nuclear translocation of cellular retinoic acid-binding protein II is regulated by retinoic acid-controlled SUMOylation J. Biol. Chem. 286 2011 42749 42757
    • (2011) J. Biol. Chem. , vol.286 , pp. 42749-42757
    • Majumdar, A.1    Petrescu, A.D.2    Xiong, Y.3    Noy, N.4
  • 25
    • 0034635958 scopus 로고    scopus 로고
    • SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage
    • Y. Mao, M. Sun, S.D. Desai, and L.F. Liu SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage Proc. Natl. Acad. Sci. USA 97 2000 4046 4051
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4046-4051
    • Mao, Y.1    Sun, M.2    Desai, S.D.3    Liu, L.F.4
  • 27
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • S. Müller, M.J. Matunis, and A. Dejean Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus EMBO J. 17 1998 61 70
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Müller, S.1    Matunis, M.J.2    Dejean, A.3
  • 30
    • 23344442009 scopus 로고    scopus 로고
    • Human MMS21/NSE2 is a SUMO ligase required for DNA repair
    • P.R. Potts, and H.T. Yu Human MMS21/NSE2 is a SUMO ligase required for DNA repair Mol. Cell. Biol. 25 2005 7021 7032
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7021-7032
    • Potts, P.R.1    Yu, H.T.2
  • 31
    • 84869091913 scopus 로고    scopus 로고
    • Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    • I. Psakhye, and S. Jentsch Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair Cell 151 2012 807 820
    • (2012) Cell , vol.151 , pp. 807-820
    • Psakhye, I.1    Jentsch, S.2
  • 32
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • M.S. Rodriguez, C. Dargemont, and R.T. Hay SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting J. Biol. Chem. 276 2001 12654 12659
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 33
    • 40649120505 scopus 로고    scopus 로고
    • Highly sensitive assays for SUMOylation and small ubiquitin-like modifier-dependent protein-protein interactions
    • N. Rouleau, J. Wang, L. Karras, E. Andrews, M. Bielefeld-Sevigny, and Y. Chen Highly sensitive assays for SUMOylation and small ubiquitin-like modifier-dependent protein-protein interactions Anal. Biochem. 375 2008 364 366
    • (2008) Anal. Biochem. , vol.375 , pp. 364-366
    • Rouleau, N.1    Wang, J.2    Karras, L.3    Andrews, E.4    Bielefeld-Sevigny, M.5    Chen, Y.6
  • 34
    • 33646031179 scopus 로고    scopus 로고
    • In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies
    • N. Saitoh, Y. Uchimura, T. Tachibana, S. Sugahara, H. Saitoh, and M. Nakao In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies Exp. Cell Res. 312 2006 1418 1430
    • (2006) Exp. Cell Res. , vol.312 , pp. 1418-1430
    • Saitoh, N.1    Uchimura, Y.2    Tachibana, T.3    Sugahara, S.4    Saitoh, H.5    Nakao, M.6
  • 35
    • 0346100493 scopus 로고    scopus 로고
    • PIAS/SUMO: New partners in transcriptional regulation
    • D. Schmidt, and S. Müller PIAS/SUMO: new partners in transcriptional regulation Cell. Mol. Life Sci. 60 2003 2561 2574
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2561-2574
    • Schmidt, D.1    Müller, S.2
  • 36
    • 33748084697 scopus 로고    scopus 로고
    • Structure-radical scavenging activity relationships of flavonoids
    • A. Seyoum, K. Asres, and F.K. El-Fiky Structure-radical scavenging activity relationships of flavonoids Phytochemistry 67 2006 2058 2070
    • (2006) Phytochemistry , vol.67 , pp. 2058-2070
    • Seyoum, A.1    Asres, K.2    El-Fiky, F.K.3
  • 39
    • 0029877917 scopus 로고    scopus 로고
    • Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine
    • S. Tsubuki, Y. Saito, M. Tomioka, H. Ito, and S. Kawashima Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine J. Biochem. 119 1996 572 576
    • (1996) J. Biochem. , vol.119 , pp. 572-576
    • Tsubuki, S.1    Saito, Y.2    Tomioka, M.3    Ito, H.4    Kawashima, S.5
  • 40
    • 59149107480 scopus 로고    scopus 로고
    • The SUMO system: An overview
    • H.D. Ulrich The SUMO system: an overview Methods Mol. Biol. 497 2009 3 16
    • (2009) Methods Mol. Biol. , vol.497 , pp. 3-16
    • Ulrich, H.D.1
  • 44
    • 0037295721 scopus 로고    scopus 로고
    • Modification with SUMO. A role in transcriptional regulation
    • A. Verger, J. Perdomo, and M. Crossley Modification with SUMO. A role in transcriptional regulation EMBO Rep. 4 2003 137 142
    • (2003) EMBO Rep. , vol.4 , pp. 137-142
    • Verger, A.1    Perdomo, J.2    Crossley, M.3
  • 45
    • 16544362972 scopus 로고    scopus 로고
    • Differential PIAS3 expression in human malignancy
    • L. Wang, and S. Banerjee Differential PIAS3 expression in human malignancy Oncol. Rep. 11 2004 1319 1324
    • (2004) Oncol. Rep. , vol.11 , pp. 1319-1324
    • Wang, L.1    Banerjee, S.2
  • 46
    • 0037452964 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier conjugation regulates nuclear export of TEL, a putative tumor suppressor
    • L.D. Wood, B.J. Irvin, G. Nucifora, K.S. Luce, and S.W. Hiebert Small ubiquitin-like modifier conjugation regulates nuclear export of TEL, a putative tumor suppressor Proc. Natl. Acad. Sci. USA 100 2003 3257 3262
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3257-3262
    • Wood, L.D.1    Irvin, B.J.2    Nucifora, G.3    Luce, K.S.4    Hiebert, S.W.5
  • 49
    • 33646353695 scopus 로고    scopus 로고
    • Assembly of a polymeric chain of SUMO1 on human topoisomerase i in vitro
    • M. Yang, C.T. Hsu, C.Y. Ting, L.F. Liu, and J. Hwang Assembly of a polymeric chain of SUMO1 on human topoisomerase I in vitro J. Biol. Chem. 281 2006 8264 8274
    • (2006) J. Biol. Chem. , vol.281 , pp. 8264-8274
    • Yang, M.1    Hsu, C.T.2    Ting, C.Y.3    Liu, L.F.4    Hwang, J.5
  • 51
    • 38549181148 scopus 로고    scopus 로고
    • Sumoylation regulates diverse biological processes
    • J. Zhao Sumoylation regulates diverse biological processes Cell. Mol. Life Sci. 64 2007 3017 3033
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 3017-3033
    • Zhao, J.1
  • 52
    • 16344370926 scopus 로고    scopus 로고
    • A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
    • X.L. Zhao, and G. Blobel A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization Proc. Natl. Acad. Sci. USA 102 2005 4777 4782
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4777-4782
    • Zhao, X.L.1    Blobel, G.2
  • 53
    • 84867397251 scopus 로고    scopus 로고
    • Discovery of a natural product inhibitor targeting protein neddylation by structure-based virtual screening
    • H.J. Zhong, V.P. Ma, Z. Cheng, D.S. Chan, H.Z. He, K.H. Leung, D.L. Ma, and C.H. Leung Discovery of a natural product inhibitor targeting protein neddylation by structure-based virtual screening Biochimie 94 2012 2457 2460
    • (2012) Biochimie , vol.94 , pp. 2457-2460
    • Zhong, H.J.1    Ma, V.P.2    Cheng, Z.3    Chan, D.S.4    He, H.Z.5    Leung, K.H.6    Ma, D.L.7    Leung, C.H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.