메뉴 건너뛰기




Volumn 111, Issue 34, 2014, Pages 12432-12437

Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli

Author keywords

Actin; Anillin; Cortactin; Listeria; Posttranslational modification

Indexed keywords

LISTERIOLYSIN O; NEDD8 PROTEIN; SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; BACTERIAL TOXIN; HEAT SHOCK PROTEIN; HEMOLYSIN; HLYA PROTEIN, LISTERIA MONOCYTOGENES; RECOMBINANT PROTEIN; SUMO PROTEIN; SUMO1 PROTEIN, HUMAN; SUMO2 PROTEIN, HUMAN;

EID: 84906695084     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1413825111     Document Type: Article
Times cited : (148)

References (41)
  • 2
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau JR, Lima CD (2010) The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition. Nat Rev Mol Cell Biol 11(12):861-871.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.12 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 3
    • 78650153662 scopus 로고    scopus 로고
    • Pathogen-mediated posttranslational modifications: A reemerging field
    • Ribet D, Cossart P (2010) Pathogen-mediated posttranslational modifications: A reemerging field. Cell 143(5):694-702.
    • (2010) Cell , vol.143 , Issue.5 , pp. 694-702
    • Ribet, D.1    Cossart, P.2
  • 4
    • 79251518045 scopus 로고    scopus 로고
    • SUMOylation and bacterial pathogens
    • Ribet D, Cossart P (2010) SUMOylation and bacterial pathogens. Virulence 1(6):532-534.
    • (2010) Virulence , vol.1 , Issue.6 , pp. 532-534
    • Ribet, D.1    Cossart, P.2
  • 5
    • 84856862707 scopus 로고    scopus 로고
    • Human pathogens and the host cell SUMOylation system
    • Wimmer P, Schreiner S, Dobner T (2012) Human pathogens and the host cell SUMOylation system. J Virol 86(2):642- 654.
    • (2012) J Virol , vol.86 , Issue.2 , pp. 642-654
    • Wimmer, P.1    Schreiner, S.2    Dobner, T.3
  • 6
    • 84876164814 scopus 로고    scopus 로고
    • Detecting endogenous SUMO targets in mammalian cells and tissues
    • Becker J, et al. (2013) Detecting endogenous SUMO targets in mammalian cells and tissues. Nat Struct Mol Biol 20(4):525-531.
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.4 , pp. 525-531
    • Becker, J.1
  • 10
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • DOI 10.1074/jbc.275.9.6252
    • Saitoh H, Hinchey J (2000) Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem 275(9):6252-6258. (Pubitemid 30129915)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.9 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 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. (2011) A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells. Mol Cell Proteomics 10(2):M110 004796.
    • (2011) Mol Cell Proteomics , vol.10 , Issue.2
    • Galisson, F.1
  • 12
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for SUMO in protein quality control
    • Tatham MH, Matic I, Mann M, Hay RT (2011) Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal 4(178):rs4.
    • (2011) Sci Signal , vol.4 , Issue.178
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 13
    • 67649173012 scopus 로고    scopus 로고
    • System-wide changes to SUMO modifications in response to heat shock
    • Golebiowski F, et al. (2009) System-wide changes to SUMO modifications in response to heat shock. Sci Signal 2(72):ra24.
    • (2009) Sci Signal , vol.2 , Issue.72
    • Golebiowski, F.1
  • 14
    • 84896387847 scopus 로고    scopus 로고
    • Uncovering SUMOylation dynamics during cell-cycle progression reveals FoxM1 as a key mitotic SUMO target protein
    • Schimmel J, et al. (2014) Uncovering SUMOylation dynamics during cell-cycle progression reveals FoxM1 as a key mitotic SUMO target protein. Mol Cell 53(6):1053-1066.
    • (2014) Mol Cell , vol.53 , Issue.6 , pp. 1053-1066
    • Schimmel, J.1
  • 15
    • 27644434674 scopus 로고    scopus 로고
    • A method of mapping protein sumoylation sites by mass spectrometry using a modified small ubiquitin-like modifier 1 (SUMO-1) and a computational program
    • DOI 10.1074/mcp.T500011-MCP200
    • Knuesel M, Cheung HT, Hamady M, Barthel KK, Liu X (2005) A method of mapping protein sumoylation sites by mass spectrometry using a modified small ubiquitin-like modifier 1 (SUMO-1) and a computational program. Mol Cell Proteomics 4(10):1626-1636. (Pubitemid 41555485)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.10 , pp. 1626-1636
    • Knuesel, M.1    Cheung, H.T.2    Hamady, M.3    Barthel, K.K.B.4    Liu, X.5
  • 16
    • 77953484491 scopus 로고    scopus 로고
    • In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification
    • Blomster HA, et al. (2010) In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification. J Biol Chem 285(25):19324-19329.
    • (2010) J Biol Chem , vol.285 , Issue.25 , pp. 19324-19329
    • Blomster, H.A.1
  • 17
    • 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. (2010) Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol Cell 39(4):641-652.
    • (2010) Mol Cell , vol.39 , Issue.4 , pp. 641-652
    • Matic, I.1
  • 18
    • 84891816010 scopus 로고    scopus 로고
    • Assay methods for small ubiquitin-like modifier (SUMO)-SUMO-interacting motif (SIM) interactions in vivo and in vitro using a split-luciferase complementation system
    • Hirohama M, et al. (2014) Assay methods for small ubiquitin-like modifier (SUMO)-SUMO-interacting motif (SIM) interactions in vivo and in vitro using a split-luciferase complementation system. Anal Biochem 448:92-94.
    • (2014) Anal Biochem , vol.448 , pp. 92-94
    • Hirohama, M.1
  • 19
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu G, Paige JS, Jaffrey SR (2010) Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat Biotechnol 28(8):868-873.
    • (2010) Nat Biotechnol , vol.28 , Issue.8 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 20
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • KimW, et al. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell 44(2):325-340.
    • (2011) Mol Cell , vol.44 , Issue.2 , pp. 325-340
    • Kim, W.1
  • 21
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • Wagner SA, et al. (2011) A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics 10(10):M111 013284.
    • (2011) Mol Cell Proteomics , vol.10 , Issue.10
    • Wagner, S.A.1
  • 22
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, et al. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1(5):376-386.
    • (2002) Mol Cell Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1
  • 23
    • 75149113118 scopus 로고    scopus 로고
    • "ChopNSpice," a mass spectrometric approach that allows identification of endogenous small ubiq-uitin- like modifier-conjugated peptides
    • Hsiao HH, Meulmeester E, Frank BT, Melchior F, Urlaub H (2009) "ChopNSpice," a mass spectrometric approach that allows identification of endogenous small ubiq-uitin- like modifier-conjugated peptides. Mol Cell Proteomics 8(12):2664 -2675.
    • (2009) Mol Cell Proteomics , vol.8 , Issue.12 , pp. 2664-2675
    • Hsiao, H.H.1    Meulmeester, E.2    Frank, B.T.3    Melchior, F.4    Urlaub, H.5
  • 24
    • 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. (2013) Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions. Mol Cell Proteomics 12(9):2536-2550.
    • (2013) Mol Cell Proteomics , vol.12 , Issue.9 , pp. 2536-2550
    • Lamoliatte, F.1
  • 25
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck PV, et al. (2012) PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res 40(Database issue):D261-D270.
    • (2012) Nucleic Acids Res , vol.40 , Issue.DATABASE ISSUE
    • Hornbeck, P.V.1
  • 26
    • 84871371484 scopus 로고    scopus 로고
    • In vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice
    • Tirard M, et al. (2012) In vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice. Proc Natl Acad Sci USA 109(51):21122-21127.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.51 , pp. 21122-21127
    • Tirard, M.1
  • 27
    • 0037163074 scopus 로고    scopus 로고
    • Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo
    • DOI 10.1074/jbc.M202780200
    • Eloranta JJ, Hurst HC (2002) Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. J Biol Chem 277(34):30798-30804. (Pubitemid 34970778)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 30798-30804
    • Eloranta, J.J.1    Hurst, H.C.2
  • 28
    • 84872413578 scopus 로고    scopus 로고
    • SUMO: A multifaceted modifier of chromatin structure and function
    • Cubeñas-Potts C, Matunis MJ (2013) SUMO: A multifaceted modifier of chromatin structure and function. Dev Cell 24(1):1-12.
    • (2013) Dev Cell , vol.24 , Issue.1 , pp. 1-12
    • Cubeñas-Potts, C.1    Matunis, M.J.2
  • 29
    • 67749097637 scopus 로고    scopus 로고
    • SUMOylation of nuclear actin
    • Hofmann WA, et al. (2009) SUMOylation of nuclear actin. J Cell Biol 186(2):193-200.
    • (2009) J Cell Biol , vol.186 , Issue.2 , pp. 193-200
    • Hofmann, W.A.1
  • 30
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensusmodification motif and nuclear targeting
    • Rodriguez MS, Dargemont C, Hay RT (2001) SUMO-1 conjugation in vivo requires both a consensusmodification motif and nuclear targeting. J Biol Chem 276(16):12654-12659.
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 31
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • Sampson DA, Wang M, Matunis MJ (2001) The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J Biol Chem 276(24):21664-21669.
    • (2001) J Biol Chem , vol.276 , Issue.24 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 32
    • 33748416853 scopus 로고    scopus 로고
    • A recurrent phospho-sumoyl switch in transcriptional repression and beyond
    • Yang XJ, Grégoire S (2006) A recurrent phospho-sumoyl switch in transcriptional repression and beyond. Mol Cell 23(6):779-786.
    • (2006) Mol Cell , vol.23 , Issue.6 , pp. 779-786
    • Yang, X.J.1    Grégoire, S.2
  • 33
    • 69949179260 scopus 로고    scopus 로고
    • A molecular basis for phosphorylation-dependent SUMO conjugation by the E2 UBC9
    • Mohideen F, et al. (2009) A molecular basis for phosphorylation-dependent SUMO conjugation by the E2 UBC9. Nat Struct Mol Biol 16(9):945- 952.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.9 , pp. 945-952
    • Mohideen, F.1
  • 35
    • 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 SH, Galanis A, Witty J, Sharrocks AD (2006) An extended consensus motif enhances the specificity of substrate modification by SUMO. EMBO J 25(21):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
  • 36
    • 83755177932 scopus 로고    scopus 로고
    • Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes
    • Cossart P (2011) Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes. Proc Natl Acad Sci USA 108(49):19484-19491.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.49 , pp. 19484-19491
    • Cossart, P.1
  • 37
    • 84864309597 scopus 로고    scopus 로고
    • Listeriolysin O: The Swiss army knife of Listeria
    • Hamon MA, Ribet D, Stavru F, Cossart P (2012) Listeriolysin O: The Swiss army knife of Listeria. Trends Microbiol 20(8):360- 368.
    • (2012) Trends Microbiol , vol.20 , Issue.8 , pp. 360-368
    • Hamon, M.A.1    Ribet, D.2    Stavru, F.3    Cossart, P.4
  • 38
    • 77951535793 scopus 로고    scopus 로고
    • Listeria monocytogenes impairs SUMOylation for efficient infection
    • Ribet D, et al. (2010) Listeria monocytogenes impairs SUMOylation for efficient infection. Nature 464(7292):1192-1195.
    • (2010) Nature , vol.464 , Issue.7292 , pp. 1192-1195
    • Ribet, D.1
  • 40
    • 84899759007 scopus 로고    scopus 로고
    • Proteome-wide identification of SUMO2 modification sites
    • Tammsalu T, et al. (2014) Proteome-wide identification of SUMO2 modification sites. Sci Signal 7(323):rs2.
    • (2014) Sci Signal , vol.7 , Issue.323
    • Tammsalu, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.