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Volumn 5, Issue , 2014, Pages

Large-scale analysis of lysine SUMOylation by SUMO remnant immunoaffinity profiling

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 2; ACTIVATING TRANSCRIPTION FACTOR 4; BLOOM SYNDROME HELICASE; CDC73 PROTEIN; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE 1; CYCLIN DEPENDENT KINASE 4; LYSINE; MONOCLONAL ANTIBODY; MYC PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEASOME; PROTEOME; SUMO PROTEIN; TRANSCRIPTION FACTOR MAF; TUMOR SUPPRESSOR PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; CDC73 PROTEIN, HUMAN; PEPTIDE;

EID: 84925341263     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6409     Document Type: Article
Times cited : (112)

References (43)
  • 1
    • 68049103216 scopus 로고    scopus 로고
    • An additional role for SUMO in ubiquitin-mediated proteolysis
    • Geoffroy, M. C. & Hay, R. T. An additional role for SUMO in ubiquitin-mediated proteolysis. Nat. Rev. Mol. Cell. Biol. 10, 564-568 (2009).
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 564-568
    • Geoffroy, M.C.1    Hay, R.T.2
  • 2
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E. S. Protein modification by SUMO. Annu. Rev. Biochem. 73, 355-382 (2004).
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 3
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M. J., Coutavas, E. & Blobel, G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135, 1457-1470 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 4
  • 6
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh, H. & Hinchey, J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275, 6252-6258 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 7
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: The SUMO proteases
    • Mukhopadhyay, D. & Dasso, M. Modification in reverse: the SUMO proteases. Trends Biochem. Sci. 32, 286-295 (2007).
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 8
    • 79955418663 scopus 로고    scopus 로고
    • Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: Sumoylation affects G-protein-coupled receptor desensitization
    • Fuhs, S. R. & Insel, P. A. Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: sumoylation affects G-protein-coupled receptor desensitization. J. Biol. Chem. 286, 14830-14841 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 14830-14841
    • Fuhs, S.R.1    Insel, P.A.2
  • 9
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham, M. H. et al. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat. Cell Biol. 10, 538-546 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 538-546
    • Tatham, M.H.1
  • 10
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9
    • Tatham, M. H. et al. Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J. Biol. Chem. 276, 35368-35374 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 35368-35374
    • Tatham, M.H.1
  • 11
    • 79953187281 scopus 로고    scopus 로고
    • A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells
    • Galisson, F. et al. A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells. Mol. Cell Proteomics 10, M110 004796 (2011).
    • (2011) Mol. Cell Proteomics , vol.10 , pp. M110
    • Galisson, F.1
  • 12
    • 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
    • Matic, I. et al. 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 (2008).
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 132-144
    • Matic, I.1
  • 13
    • 4043051557 scopus 로고    scopus 로고
    • A proteomic study of SUMO-2 target proteins
    • Vertegaal, A. C. et al. A proteomic study of SUMO-2 target proteins. J. Biol. Chem. 279, 33791-33798 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 33791-33798
    • Vertegaal, A.C.1
  • 14
    • 15944414509 scopus 로고    scopus 로고
    • A proteomic strategy for gaining insights into protein sumoylation in yeast
    • Denison, C. et al. A proteomic strategy for gaining insights into protein sumoylation in yeast. Mol. Cell Proteomics 4, 246-254 (2005).
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 246-254
    • Denison, C.1
  • 15
    • 14244260623 scopus 로고    scopus 로고
    • Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae
    • Hannich, J. T. et al. Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae. J. Biol. Chem. 280, 4102-4110 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 4102-4110
    • Hannich, J.T.1
  • 16
    • 4744360999 scopus 로고    scopus 로고
    • A proteome-wide approach identifies sumoylated substrate proteins in yeast
    • Panse, V. G., Hardeland, U., Werner, T., Kuster, B. & Hurt, E. A proteome-wide approach identifies sumoylated substrate proteins in yeast. J. Biol. Chem. 279, 41346-41351 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 41346-41351
    • Panse, V.G.1    Hardeland, U.2    Werner, T.3    Kuster, B.4    Hurt, E.5
  • 17
    • 67650115041 scopus 로고    scopus 로고
    • Genetic and proteomic evidence for roles of Drosophila SUMO in cell cycle control, Ras signaling, and early pattern formation
    • Nie, M., Xie, Y., Loo, J. A. & Courey, A. J. Genetic and proteomic evidence for roles of Drosophila SUMO in cell cycle control, Ras signaling, and early pattern formation. PLoS ONE 4, e5905 (2009).
    • (2009) PLoS ONE , vol.4
    • Nie, M.1    Xie, Y.2    Loo, J.A.3    Courey, A.J.4
  • 18
    • 78049235116 scopus 로고    scopus 로고
    • Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis
    • Miller, M. J., Barrett-Wilt, G. A., Hua, Z. & Vierstra, R. D. Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis. Proc. Natl Acad. Sci. USA 107, 16512-16517 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 16512-16517
    • Miller, M.J.1    Barrett-Wilt, G.A.2    Hua, Z.3    Vierstra, R.D.4
  • 19
    • 67649173012 scopus 로고    scopus 로고
    • System-wide changes to SUMO modifications in response to heat shock
    • Golebiowski, F. et al. System-wide changes to SUMO modifications in response to heat shock. Sci. Signal. 2, ra24 (2009).
    • (2009) Sci. Signal , vol.2 , pp. ra24
    • Golebiowski, F.1
  • 20
    • 71049147061 scopus 로고    scopus 로고
    • Proteomics analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition
    • Matafora, V., D'Amato, A., Mori, S., Blasi, F. & Bachi, A. Proteomics analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition. Mol. Cell. Proteomics 8, 2243-2255 (2009).
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2243-2255
    • Matafora, V.1    D'Amato, A.2    Mori, S.3    Blasi, F.4    Bachi, A.5
  • 21
    • 33846019234 scopus 로고    scopus 로고
    • Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics
    • Vertegaal, A. C. et al. Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol. Cell. Proteomics 5, 2298-2310 (2006).
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2298-2310
    • Vertegaal, A.C.1
  • 22
    • 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. et al. 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).
    • (2010) Mol. Cell , vol.39 , pp. 641-652
    • Matic, I.1
  • 23
    • 84863011119 scopus 로고    scopus 로고
    • Analysis of oxygen/glucose-deprivation-induced changes in SUMO3 conjugation using SILAC-based quantitative proteomics
    • Yang, W. et al. Analysis of oxygen/glucose-deprivation-induced changes in SUMO3 conjugation using SILAC-based quantitative proteomics. J. Proteome Res. 11, 1108-1117 (2012).
    • (2012) J. Proteome Res. , vol.11 , pp. 1108-1117
    • Yang, W.1
  • 24
    • 3543018486 scopus 로고    scopus 로고
    • Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses
    • Zhou, W., Ryan, J. J. & Zhou, H. Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses. J. Biol. Chem. 279, 32262-32268 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 32262-32268
    • Zhou, W.1    Ryan, J.J.2    Zhou, H.3
  • 25
    • 79551604903 scopus 로고    scopus 로고
    • Purification and identification of endogenous polySUMO conjugates
    • Bruderer, R. et al. Purification and identification of endogenous polySUMO conjugates. EMBO Rep. 12, 142-148 (2011).
    • (2011) EMBO Rep. , vol.12 , pp. 142-148
    • Bruderer, R.1
  • 26
    • 84876164814 scopus 로고    scopus 로고
    • Detecting endogenous SUMO targets in mammalian cells and tissues
    • Becker, J. et al. Detecting endogenous SUMO targets in mammalian cells and tissues. Nat. Struct. Mol. Biol. 20, 525-531 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 525-531
    • Becker, J.1
  • 27
    • 33745360876 scopus 로고    scopus 로고
    • Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software
    • Pedrioli, P. G. et al. Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software. Nat. Methods 3, 533-539 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 533-539
    • Pedrioli, P.G.1
  • 28
    • 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. & Urlaub, H. 'ChopNSpice,' a mass spectrometric approach that allows identification of endogenous small ubiquitin-like modifier-conjugated peptides. Mol. Cell. Proteomics 8, 2664-2675 (2009).
    • (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
  • 29
    • 11844269891 scopus 로고    scopus 로고
    • The parafibromin tumor suppressor protein is part of a human Paf1 complex
    • Rozenblatt-Rosen, O. et al. The parafibromin tumor suppressor protein is part of a human Paf1 complex. Mol. Cell. Biol. 25, 612-620 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 612-620
    • Rozenblatt-Rosen, O.1
  • 30
    • 84884376262 scopus 로고    scopus 로고
    • Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions
    • Lamoliatte, F. et al. Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions. Mol. Cell. Proteomics 12, 2536-2550 (2013).
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 2536-2550
    • Lamoliatte, F.1
  • 31
    • 57049091711 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system is a key component of the SUMO-2/3 cycle
    • Schimmel, J. et al. The ubiquitin-proteasome system is a key component of the SUMO-2/3 cycle. Mol. Cell. Proteomics 7, 2107-2122 (2008).
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2107-2122
    • Schimmel, J.1
  • 32
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz, D. & Gygi, S. P. An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotechnol. 23, 1391-1398 (2005).
    • (2005) Nat. Biotechnol , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 33
    • 33750439105 scopus 로고    scopus 로고
    • An extended consensus motif enhances the specificity of substrate modification by SUMO
    • Yang, S. H., Galanis, A., Witty, J. & Sharrocks, A. D. An extended consensus motif enhances the specificity of substrate modification by SUMO. EMBO. J. 25, 5083-5093 (2006).
    • (2006) EMBO. J , vol.25 , pp. 5083-5093
    • Yang, S.H.1    Galanis, A.2    Witty, J.3    Sharrocks, A.D.4
  • 34
    • 30444440554 scopus 로고    scopus 로고
    • PDSM, a motif for phosphorylation-dependent SUMO modification
    • Hietakangas, V. et al. PDSM, a motif for phosphorylation-dependent SUMO modification. Proc. Natl Acad. Sci. USA 103, 45-50 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 45-50
    • Hietakangas, V.1
  • 35
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for SUMO in protein quality control
    • Tatham, M. H., Matic, I., Mann, M. & Hay, R. T. Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci. Signal. 4, rs4 (2011).
    • (2011) Sci. Signal , vol.4 , pp. rs4
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 36
    • 79959861920 scopus 로고    scopus 로고
    • SHP2 tyrosine phosphatase converts parafibromin/Cdc73 from a tumor suppressor to an oncogenic driver
    • Takahashi, A. et al. SHP2 tyrosine phosphatase converts parafibromin/Cdc73 from a tumor suppressor to an oncogenic driver. Mol. Cell 43, 45-56 (2011).
    • (2011) Mol. Cell , vol.43 , pp. 45-56
    • Takahashi, A.1
  • 37
    • 84899759007 scopus 로고    scopus 로고
    • Proteome-wide identification of SUMO2 modification sites
    • Tammsalu, T. et al. Proteome-wide identification of SUMO2 modification sites. Sci. Signal. 7, rs2 (2014).
    • (2014) Sci. Signal , vol.7 , pp. rs2
    • Tammsalu, T.1
  • 38
    • 84874619400 scopus 로고    scopus 로고
    • Refined preparation and use of anti-diglycine remnant (K-epsilon-GG) antibody enables routine quantification of 10,000 s of ubiquitination sites in single proteomics experiments
    • Udeshi, N. D. et al. Refined preparation and use of anti-diglycine remnant (K-epsilon-GG) antibody enables routine quantification of 10,000 s of ubiquitination sites in single proteomics experiments. Mol. Cell. Proteomics 12, 825-831 (2013).
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 825-831
    • Udeshi, N.D.1
  • 39
    • 84904461202 scopus 로고    scopus 로고
    • Interplay between nuclear transport and ubiquitin/SUMO modifications in the regulation of cancer-related proteins
    • Rodriguez, J. A. Interplay between nuclear transport and ubiquitin/SUMO modifications in the regulation of cancer-related proteins. Semin. Cancer Biol. 27C, 11-19 (2014).
    • (2014) Semin. Cancer Biol. , vol.27 C , pp. 11-19
    • Rodriguez, J.A.1
  • 40
    • 84871117932 scopus 로고    scopus 로고
    • Sumoylation of SAE2 C terminus regulates SAE nuclear localization
    • Truong, K., Lee, T. D., Li, B. & Chen, Y. Sumoylation of SAE2 C terminus regulates SAE nuclear localization. J. Biol. Chem. 287, 42611-42619 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 42611-42619
    • Truong, K.1    Lee, T.D.2    Li, B.3    Chen, Y.4
  • 41
    • 84866510150 scopus 로고    scopus 로고
    • Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms
    • Maroui, M. A. et al. Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms. PLoS ONE 7, e44949 (2012).
    • (2012) PLoS ONE , vol.7
    • Maroui, M.A.1
  • 42
    • 33645731673 scopus 로고    scopus 로고
    • A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling
    • Dantuma, N. P., Groothuis, T. A., Salomons, F. A. & Neefjes, J. A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling. J. Cell Biol. 173, 19-26 (2006).
    • (2006) J. Cell Biol. , vol.173 , pp. 19-26
    • Dantuma, N.P.1    Groothuis, T.A.2    Salomons, F.A.3    Neefjes, J.4
  • 43
    • 42649142332 scopus 로고    scopus 로고
    • Combined enzymatic and data mining approaches for comprehensive phosphoproteome analyses: Application to cell signaling events of interferon-gamma-stimulated macrophages
    • Marcantonio, M., Trost, M., Courcelles, M., Desjardins, M. & Thibault, P. 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 (2008).
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 645-660
    • Marcantonio, M.1    Trost, M.2    Courcelles, M.3    Desjardins, M.4    Thibault, P.5


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