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Volumn 12, Issue 9, 2013, Pages 2536-2550

Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DNA; LYSINE; SUMO PROTEIN; SYNTHETIC PEPTIDE; TRYPSIN; UBIQUITIN;

EID: 84884376262     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.025569     Document Type: Article
Times cited : (39)

References (36)
  • 1
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • DOI 10.1016/j.molcel.2005.03.012
    • Hay, R. T. (2005) SUMO: a history of modification. Mol Cell 18, 1-12 (Pubitemid 40444643)
    • (2005) Molecular Cell , vol.18 , Issue.1 , pp. 1-12
    • Hay, R.T.1
  • 2
    • 76449110686 scopus 로고    scopus 로고
    • Diversity of the sumoylation machinery in plants
    • Lois, L. M. (2010) Diversity of the SUMOylation machinery in plants. Biochem. Soc Trans 38, 60-64
    • (2010) Biochem. Soc Trans , vol.38 , pp. 60-64
    • Lois, L.M.1
  • 4
    • 34248338373 scopus 로고    scopus 로고
    • Sumo: Regulating the regulator
    • Bossis, G., and Melchior, F. (2006) SUMO: regulating the regulator. Cell Div 1, 13
    • (2006) Cell Div , vol.1 , pp. 13
    • Bossis, G.1    Melchior, F.2
  • 5
    • 42049108221 scopus 로고    scopus 로고
    • Cell biology: SUMO
    • DOI 10.1038/452709a, PII 452709A
    • Meulmeester, E., and Melchior, F. (2008) Cell biology: SUMO. Nature 452, 709-711 (Pubitemid 351521073)
    • (2008) Nature , vol.452 , Issue.7188 , pp. 709-711
    • Meulmeester, E.1    Melchior, F.2
  • 6
  • 7
    • 0035918226 scopus 로고    scopus 로고
    • Sumo-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez, M. S., Dargemont, C., and Hay, R. T. (2001) SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem. 276, 12654-12659
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 9
    • 33750439105 scopus 로고    scopus 로고
    • An extended consensus motif enhances the specificity of substrate modification by SUMO
    • DOI 10.1038/sj.emboj.7601383, PII 7601383
    • Yang, S. H., Galanis, A., Witty, J., and Sharrocks, A. D. (2006) An extended consensus motif enhances the specificity of substrate modification by SUMO. EMBO J. 25, 5083-5093 (Pubitemid 44658526)
    • (2006) EMBO Journal , vol.25 , Issue.21 , pp. 5083-5093
    • Yang, S.-H.1    Galanis, A.2    Witty, J.3    Sharrocks, A.D.4
  • 11
    • 1542501958 scopus 로고    scopus 로고
    • SUMO: Ligases, isopeptidases and nuclear pores
    • DOI 10.1016/j.tibs.2003.09.002, PII S0968000403002263
    • Melchior, F., Schergaut, M., and Pichler, A. (2003) SUMO: ligases, isopeptidases and nuclear pores. Trends Biochem. Sci 28, 612-618 (Pubitemid 38352808)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.11 , pp. 612-618
    • Melchior, F.1    Schergaut, M.2    Pichler, A.3
  • 12
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: The SUMO proteases
    • DOI 10.1016/j.tibs.2007.05.002, PII S0968000407001223
    • Mukhopadhyay, D., and Dasso, M. (2007) Modification in reverse: the SUMO proteases. Trends Biochem. Sci 32, 286-295 (Pubitemid 46874931)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.6 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 15
    • 33846019234 scopus 로고    scopus 로고
    • Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics
    • DOI 10.1074/mcp.M600212-MCP200
    • Vertegaal, A. C., Andersen, J. S., Ogg, S. C., Hay, R. T., Mann, M., and Lamond, A. I. (2006) Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol Cell Proteomics 5, 2298-2310 (Pubitemid 46040634)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.12 , pp. 2298-2310
    • Vertegaal, A.C.O.1    Andersen, J.S.2    Ogg, S.C.3    Hay, R.T.4    Mann, M.5    Lamond, A.I.6
  • 16
    • 33745360876 scopus 로고    scopus 로고
    • Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software
    • DOI 10.1038/nmeth891, PII N891
    • Pedrioli, P. G., Raught, B., Zhang, X. D., Rogers, R., Aitchison, J., Matunis, M., and Aebersold, R. (2006) Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software. Nat Methods 3, 533-539 (Pubitemid 43941771)
    • (2006) Nature Methods , vol.3 , Issue.7 , pp. 533-539
    • Pedrioli, P.G.A.1    Raught, B.2    Zhang, X.-D.3    Rogers, R.4    Aitchison, J.5    Matunis, M.6    Aebersold, R.7
  • 17
    • 75149113118 scopus 로고    scopus 로고
    • Chopnspice, a mass spectrometric approach that allows identification of endogenous small ubiquitin-like modifier-conjugated peptides
    • Hsiao, H. H., Meulmeester, E., Frank, B. T., Melchior, F., and Urlaub, H. (2009) "ChopNSpice," a mass spectrometric approach that allows identification of endogenous small ubiquitin-like modifier-conjugated peptides. Mol Cell Proteomics 8, 2664-2675
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2664-2675
    • Hsiao, H.H.1    Meulmeester, E.2    Frank, B.T.3    Melchior, F.4    Urlaub, H.5
  • 19
    • 77955999636 scopus 로고    scopus 로고
    • Site-specific identification of sumo-2 targets in cells reveals an inverted sumoylation motif and a hydrophobic cluster sumoylation motif
    • Matic, I., Schimmel, J., Hendriks, I. A., van Santen, M. A., van de Rijke, F., van Dam, H., Gnad, F., Mann, M., and Vertegaal, A. C. (2010) Site-Specific Identification of SUMO-2 Targets in Cells Reveals an Inverted SUMOylation Motif and a Hydrophobic Cluster SUMOylation Motif. Mol. Cell 39, 641-652
    • (2010) Mol. Cell , vol.39 , pp. 641-652
    • Matic, I.1    Schimmel, J.2    Hendriks, I.A.3    Van Santen, M.A.4    Van De Rijke, F.5    Van Dam, H.6    Gnad, F.7    Mann, M.8    Vertegaal, A.C.9
  • 20
    • 84861860481 scopus 로고    scopus 로고
    • Targeted data extraction of the ms/ms spectra generated by data-independent acquisition: A new concept for consistent and accurate proteome analysis
    • Gillet, L. C., Navarro, P., Tate, S., Röst, H., Selevsek, N., Reiter, L., Bonner, R., and Aebersold, R. (2012) Targeted data extraction of the MS/MS spectra generated by data-independent acquisition: a new concept for consistent and accurate proteome analysis. Mol. Cell. Proteomics 11, O111016717
    • (2012) Mol. Cell. Proteomics , vol.11
    • Gillet, L.C.1    Navarro, P.2    Tate, S.3    Röst, H.4    Selevsek, N.5    Reiter, L.6    Bonner, R.7    Aebersold, R.8
  • 21
    • 0026656122 scopus 로고
    • Spot-synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support
    • Frank, F. (1992) Spot-synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron 48, 9217-9232
    • (1992) Tetrahedron , vol.48 , pp. 9217-9232
    • Frank, F.1
  • 22
    • 42649142332 scopus 로고    scopus 로고
    • Combined enzymatic and data mining approaches for comprehensive phosphoproteome analyses: Application to cell signaling events of interferon-γ-stimulated macrophages
    • DOI 10.1074/mcp.M700383-MCP200
    • Marcantonio, M., Trost, M., Courcelles, M., Desjardins, M., and Thibault, P. (2008) Combined enzymatic and data mining approaches for comprehensive phosphoproteome analyses: application to cell signaling events of interferon-gamma-stimulated macrophages. Mol. Cell. Proteomics 7, 645-660 (Pubitemid 351597477)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.4 , pp. 645-660
    • Marcantonio, M.1    Trost, M.2    Courcelles, M.3    Desjardins, M.4    Thibault, P.5
  • 23
    • 4544368228 scopus 로고    scopus 로고
    • 1 fragment ions in collision-induced dissociation of glutamine-containing peptide ions: A tip for de novo sequencing
    • DOI 10.1002/rcm.1593
    • Lee, Y. J., and Lee, Y. M. (2004) Formation of c(1) fragment ions in collision-induced dissociation of glutamine-containing peptide ions: a tip for de novo sequencing. Rapid Commun. Mass Spectrom. 18, 2069-2076 (Pubitemid 39222448)
    • (2004) Rapid Communications in Mass Spectrometry , vol.18 , Issue.18 , pp. 2069-2076
    • Lee, Y.J.1    Lee, Y.M.2
  • 24
    • 77957990113 scopus 로고    scopus 로고
    • Proteomics on an orbitrap benchtop mass spectrometer using all-ion fragmentation
    • Geiger, T., Cox, J., and Mann, M. (2010) Proteomics on an Orbitrap benchtop mass spectrometer using all-ion fragmentation. Mol. Cell. Proteomics 9, 2252-2261
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2252-2261
    • Geiger, T.1    Cox, J.2    Mann, M.3
  • 25
    • 0038047154 scopus 로고    scopus 로고
    • Shotgun collision-induced dissociation of peptides using a time of flight mass analyzer
    • DOI 10.1002/pmic.200300362
    • Purvine, S., Eppel, J. T., Yi, E. C., and Goodlett, D. R. (2003) Shotgun collision-induced dissociation of peptides using a time of flight mass analyzer. Proteomics 3, 847-850 (Pubitemid 36801670)
    • (2003) Proteomics , vol.3 , Issue.6 , pp. 847-850
    • Purvine, S.1    Eppel, J.-T.2    Yi, E.C.3    Goodlett, D.R.4
  • 27
    • 14744293536 scopus 로고    scopus 로고
    • Automated approach for quantitative analysis of complex peptide mixtures from tandem mass spectra
    • Venable, J. D., Dong, M. Q., Wohlschlegel, J., Dillin, A., and Yates, J. R. (2004) Automated approach for quantitative analysis of complex peptide mixtures from tandem mass spectra. Nat. Methods 1, 39-45
    • (2004) Nat. Methods , vol.1 , pp. 39-45
    • Venable, J.D.1    Dong, M.Q.2    Wohlschlegel, J.3    Dillin, A.4    Yates, J.R.5
  • 30
    • 26444593473 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: Identification of lysines in RanBP2 and SUMO targeted for modification during the E3 autoSUMOylation reaction
    • DOI 10.1021/ac058019d
    • Cooper, H. J., Tatham, M. H., Jaffray, E., Heath, J. K., Lam, T. T., Marshall, A. G., and Hay, R. T. (2005) Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: identification of lysines in RanBP2 and SUMO targeted for modification during the E3 autoSUMOylation reaction. Anal. Chem. 77, 6310-6319 (Pubitemid 41436967)
    • (2005) Analytical Chemistry , vol.77 , Issue.19 , pp. 6310-6319
    • Cooper, H.J.1    Tatham, M.H.2    Jaffray, E.3    Heath, J.K.4    Lam, T.T.5    Marshall, A.G.6    Hay, R.T.7
  • 31
    • 39049093685 scopus 로고    scopus 로고
    • In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy
    • DOI 10.1074/mcp.M700173-MCP200
    • Matic, I., van Hagen, M., Schimmel, J., Macek, B., Ogg, S. C., Tatham, M. H., Hay, R. T., Lamond, A. I., Mann, M., and Vertegaal, A. C. (2008) In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. Mol. Cell. Proteomics 7, 132-144 (Pubitemid 351248239)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.1 , pp. 132-144
    • Matic, I.1    Van Hagen, M.2    Schimmel, J.3    Macek, B.4    Ogg, S.C.5    Tatham, M.H.6    Hay, R.T.7    Lamond, A.I.8    Mann, M.9    Vertegaal, A.C.O.10
  • 33
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PML-RARα through a SUMO-triggered RNF4/ ubiquitin-mediated pathway
    • DOI 10.1038/ncb1717, PII NCB1717
    • Lallemand-Breitenbach, V., Jeanne, M., Benhenda, S., Nasr, R., Lei, M., Peres, L., Zhou, J., Zhu, J., Raught, B., and de Thé, H. (2008) Arsenic degrades PML or PML-RARalpha through a SUMO-Triggered RNF4/ubiquitin-mediated pathway. Nat. Cell Biol. 10, 547-555 (Pubitemid 351627374)
    • (2008) Nature Cell Biology , vol.10 , Issue.5 , pp. 547-555
    • Lallemand-Breitenbach, V.1    Jeanne, M.2    Benhenda, S.3    Nasr, R.4    Lei, M.5    Peres, L.6    Zhou, J.7    Raught, B.8
  • 34
    • 76449116924 scopus 로고    scopus 로고
    • Sumo in the mammalian response to dna damage
    • Morris, J. R. (2010) SUMO in the mammalian response to DNA damage. Biochem. Soc. Trans. 38, 92-97
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 92-97
    • Morris, J.R.1
  • 35
    • 80052765356 scopus 로고    scopus 로고
    • Sumoylation and de-sumoylation in response to dna damage
    • Dou, H., Huang, C., Van Nguyen, T., Lu, L. S., and Yeh, E. T. (2011) SUMOylation and de-SUMOylation in response to DNA damage. FEBS Lett. 585, 2891-2896
    • (2011) FEBS Lett. , vol.585 , pp. 2891-2896
    • Dou, H.1    Huang, C.2    Van Nguyen, T.3    Lu, L.S.4    Yeh, E.T.5
  • 36
    • 1842457017 scopus 로고    scopus 로고
    • RanGAP1SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly
    • DOI 10.1083/jcb.200309126
    • Swaminathan, S., Kiendl, F., Körner, R., Lupetti, R., Hengst, L., and Melchior, F. (2004) RanGAP1 SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly. J. Cell Biol. 164, 965-971 (Pubitemid 38429122)
    • (2004) Journal of Cell Biology , vol.164 , Issue.7 , pp. 965-971
    • Swaminathan, S.1    Kiendl, F.2    Korner, R.3    Lupetti, R.4    Hengst, L.5    Melchior, F.6


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