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Volumn 5 S, Issue 2, 2013, Pages 544-553

Sumo paralogs: Redundancy and divergencies

Author keywords

Desumoylases; E3 ligases; Paralog specificity; Review; SIMs; SUMO1; SUMO2 3; SUMO4

Indexed keywords

BASIC LEUCINE ZIPPER TRANSCRIPTION FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HISTONE DEACETYLASE 4; RECQ HELICASE; RING FINGER PROTEIN; SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; SUMO 4 PROTEIN; SUMO PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84884333239     PISSN: 19450516     EISSN: 19450524     Source Type: Journal    
DOI: 10.2741/s388     Document Type: Article
Times cited : (34)

References (84)
  • 2
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-sumo crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • E. Mossessova and C. D. Lima: Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol Cell, 5(5), 865-76 (2000)
    • (2000) Mol Cell , vol.5 , Issue.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 3
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for e2-mediated sumo conjugation revealed by a complex between ubiquitin conjugating enzyme ubc9 and rangap1
    • V. Bernier-Villamor, D. A. Sampson, M. J. Matunis and C. D. Lima: Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin conjugating enzyme Ubc9 and RanGAP1. Cell, 108(3), 345-56 (2002)
    • (2002) Cell , vol.108 , Issue.3 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 4
    • 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(16), 12654-9 (2001)
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 5
    • 3042644131 scopus 로고    scopus 로고
    • A m55v polymorphism in a novel sumo gene (sumo-4) differentially activates heat shock transcription factors and is associated with susceptibility to type i diabetes mellitus
    • K. M. Bohren, V. Nadkarni, J. H. Song, K. H. Gabbay and D. Owerbach: A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus. J Biol Chem, 279(26), 27233-8 (2004)
    • (2004) J Biol Chem , vol.279 , Issue.26 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.2    Song, J.H.3    Gabbay, K.H.4    Owerbach, D.5
  • 6
    • 7044269671 scopus 로고    scopus 로고
    • Crystal structures of the human sumo-2 protein at 1.6 a and 1.2 a resolution: Implication on the functional differences of sumo proteins
    • W. C. Huang, T. P. Ko, S. S. Li and A. H. Wang: Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins. Eur J Biochem, 271(20), 4114-22 (2004)
    • (2004) Eur J Biochem , vol.271 , Issue.20 , pp. 4114-4122
    • Huang, W.C.1    Ko, T.P.2    Li, S.S.3    Wang, A.H.4
  • 8
    • 33745360876 scopus 로고    scopus 로고
    • Automated identification of sumoylation sites using mass spectrometry and summon pattern recognition software
    • P. G. Pedrioli, B. Raught, X. D. Zhang, R. Rogers, J. Aitchison, M. Matunis and R. Aebersold: Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software. Nat Methods, 3(7), 533-9 (2006)
    • (2006) Nat Methods , vol.3 , Issue.7 , pp. 533-539
    • Pedrioli, P.G.1    Raught, B.2    Zhang, X.D.3    Rogers, R.4    Aitchison, J.5    Matunis, M.6    Aebersold, R.7
  • 9
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric chains of sumo-2 and sumo-3 are conjugated to protein substrates by sae1/sae2 and ubc9
    • M. H. Tatham, E. Jaffray, O. A. Vaughan, J. M. Desterro, C. H. Botting, J. H. Naismith and R. T. Hay: Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J Biol Chem, 276(38), 35368-74 (2001)
    • (2001) J Biol Chem , vol.276 , Issue.38 , pp. 35368-35374
    • Tatham, M.H.1    Jaffray, E.2    Vaughan, O.A.3    Desterro, J.M.4    Botting, C.H.5    Naismith, J.H.6    Hay, R.T.7
  • 10
    • 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
    • I. Matic, M. van Hagen, J. Schimmel, B. Macek, S. C. Ogg, M. H. Tatham, R. T. Hay, A. I. Lamond, M. Mann and A. C. Vertegaal: 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(1), 132-44 (2008)
    • (2008) Mol Cell 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.10
  • 11
    • 77953484491 scopus 로고    scopus 로고
    • In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification
    • H. A. Blomster, S. Y. Imanishi, J. Siimes, J. Kastu, N. A. Morrice, J. E. Eriksson and L. Sistonen: In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification. J Biol Chem, 285(25), 19324-9 (2010)
    • (2010) J Biol Chem , vol.285 , Issue.25 , pp. 19324-19329
    • Blomster, H.A.1    Imanishi, S.Y.2    Siimes, J.3    Kastu, J.4    Morrice, N.A.5    Eriksson, J.E.6    Sistonen, L.7
  • 13
    • 0029736651 scopus 로고    scopus 로고
    • Pic 1, a novel ubiquitin-like protein which interacts with the pml component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • M. N. Boddy, K. Howe, L. D. Etkin, E. Solomon and P. S. Freemont: PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene, 13(5), 971-82 (1996)
    • (1996) Oncogene , vol.13 , Issue.5 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 14
    • 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
    • M. J. Matunis, E. Coutavas and G. Blobel: 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(6 Pt 1), 1457-70 (1996)
    • (1996) J Cell Biol , vol.135 , Issue.6 PART 1 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 15
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting rangap1 to nuclear pore complex protein ranbp2
    • R. Mahajan, C. Delphin, T. Guan, L. Gerace and F. Melchior: A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell, 88(1), 97-107 (1997)
    • (1997) Cell , vol.88 , Issue.1 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 16
    • 9444260454 scopus 로고    scopus 로고
    • Distinct in vivo dynamics of vertebrate sumo paralogues
    • F. Ayaydin and M. Dasso: Distinct in vivo dynamics of vertebrate SUMO paralogues. Mol Biol Cell, 15(12), 5208-18 (2004)
    • (2004) Mol Biol Cell , vol.15 , Issue.12 , pp. 5208-5218
    • Ayaydin, F.1    Dasso, M.2
  • 17
    • 0035576878 scopus 로고    scopus 로고
    • Piasy, a nuclear matrix-associated sumo e3 ligase, represses lef1 activity by sequestration into nuclear bodies
    • S. Sachdev, L. Bruhn, H. Sieber, A. Pichler, F. Melchior and R. Grosschedl: PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes & development, 15(23), 3088-103 (2001)
    • (2001) Genes & development , vol.15 , Issue.23 , pp. 3088-3103
    • Sachdev, S.1    Bruhn, L.2    Sieber, H.3    Pichler, A.4    Melchior, F.5    Grosschedl, R.6
  • 19
    • 20444384040 scopus 로고    scopus 로고
    • Insights into e3 ligase activity revealed by a sumo-rangap1-ubc9-nup358 complex
    • D. Reverter and C. D. Lima: Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature, 435(7042), 687-92 (2005)
    • (2005) Nature , vol.435 , Issue.7042 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 20
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein pc2 is a sumo e3
    • M. H. Kagey, T. A. Melhuish and D. Wotton: The polycomb protein Pc2 is a SUMO E3. Cell, 113(1), 127-37 (2003)
    • (2003) Cell , vol.113 , Issue.1 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 21
    • 25444462980 scopus 로고    scopus 로고
    • Regulation of mef2 by histone deacetylase 4-and sirt1 deacetylase-mediated lysine modifications
    • X. Zhao, T. Sternsdorf, T. A. Bolger, R. M. Evans and T. P. Yao: Regulation of MEF2 by histone deacetylase 4-and SIRT1 deacetylase-mediated lysine modifications. Mol Cell Biol, 25(19), 8456-64 (2005)
    • (2005) Mol Cell Biol , vol.25 , Issue.19 , pp. 8456-8464
    • Zhao, X.1    Sternsdorf, T.2    Bolger, T.A.3    Evans, R.M.4    Yao, T.P.5
  • 22
    • 24144483441 scopus 로고    scopus 로고
    • Topors acts as a sumo-1 e3 ligase for p53 in vitro and in vivo
    • S. Weger, E. Hammer and R. Heilbronn: Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo. FEBS Lett, 579(22), 5007-12 (2005)
    • (2005) FEBS Lett , vol.579 , Issue.22 , pp. 5007-5012
    • Weger, S.1    Hammer, E.2    Heilbronn, R.3
  • 23
    • 66749167799 scopus 로고    scopus 로고
    • Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity
    • S. Subramaniam, K. M. Sixt, R. Barrow and S. H. Snyder: Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity. Science, 324(5932), 1327-30 (2009)
    • (2009) Science , vol.324 , Issue.5932 , pp. 1327-1330
    • Subramaniam, S.1    Sixt, K.M.2    Barrow, R.3    Snyder, S.H.4
  • 24
    • 79952281303 scopus 로고    scopus 로고
    • Sumo e3 ligase activity of trim proteins
    • Y. Chu and X. Yang: SUMO E3 ligase activity of TRIM proteins. Oncogene, 30(9), 1108-16 (2011)
    • (2011) Oncogene , vol.30 , Issue.9 , pp. 1108-1116
    • Chu, Y.1    Yang, X.2
  • 26
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers sumo-1 versus sumo-2/3
    • H. Saitoh and J. Hinchey: Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem, 275(9), 6252-8 (2000)
    • (2000) J Biol Chem , vol.275 , Issue.9 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 27
    • 0242509262 scopus 로고    scopus 로고
    • Sumo-2/3 regulates topoisomerase ii in mitosis
    • Y. Azuma, A. Arnaoutov and M. Dasso: SUMO-2/3 regulates topoisomerase II in mitosis. J Cell Biol, 163(3), 477-487 (2003)
    • (2003) J Cell Biol , vol.163 , Issue.3 , pp. 477-487
    • Azuma, Y.1    Arnaoutov, A.2    Dasso, M.3
  • 28
    • 0033037274 scopus 로고    scopus 로고
    • Pic-1/sumo-1-modified pml-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia
    • T. Sternsdorf, E. Puccetti, K. Jensen, D. Hoelzer, H. Will, O. G. Ottmann and M. Ruthardt: PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. Mol Cell Biol, 19(7), 5170-8 (1999)
    • (1999) Mol Cell Biol , vol.19 , Issue.7 , pp. 5170-5178
    • Sternsdorf, T.1    Puccetti, E.2    Jensen, K.3    Hoelzer, D.4    Will, H.5    Ottmann, O.G.6    Ruthardt, M.7
  • 29
    • 15644368249 scopus 로고    scopus 로고
    • Covalent modification of pml by the sentrin family of ubiquitin-like proteins
    • T. Kamitani, H. P. Nguyen, K. Kito, T. Fukuda-Kamitani and E. T. Yeh: Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J Biol Chem, 273(6), 3117-20 (1998)
    • (1998) J Biol Chem , vol.273 , Issue.6 , pp. 3117-3120
    • Kamitani, T.1    Nguyen, H.P.2    Kito, K.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 30
    • 14644402420 scopus 로고    scopus 로고
    • A universal strategy for proteomic studies of sumo and other ubiquitin-like modifiers
    • G. Rosas-Acosta, W. K. Russell, A. Deyrieux, D. H. Russell and V. G. Wilson: A universal strategy for proteomic studies of SUMO and other ubiquitin-like modifiers. Mol Cell Proteomics, 4(1), 56-72 (2005)
    • (2005) Mol Cell Proteomics , vol.4 , Issue.1 , pp. 56-72
    • Rosas-Acosta, G.1    Russell, W.K.2    Deyrieux, A.3    Russell, D.H.4    Wilson, V.G.5
  • 31
    • 33846019234 scopus 로고    scopus 로고
    • Distinct and overlapping sets of sumo-1 and sumo-2 target proteins revealed by quantitative proteomics
    • A. C. Vertegaal, J. S. Andersen, S. C. Ogg, R. T. Hay, M. Mann and A. I. Lamond: Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol Cell Proteomics, 5(12), 2298-310 (2006)
    • (2006) Mol Cell Proteomics , vol.5 , Issue.12 , pp. 2298-2310
    • Vertegaal, A.C.1    Andersen, J.S.2    Ogg, S.C.3    Hay, R.T.4    Mann, M.5    Lamond, A.I.6
  • 32
    • 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
    • D. A. Sampson, M. Wang and M. J. Matunis: 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), 21664-9 (2001)
    • (2001) J Biol Chem , vol.276 , Issue.24 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 33
    • 28844455305 scopus 로고    scopus 로고
    • Small ubiquitinlike modifier (sumo) recognition of a sumo binding motif: A reversal of the bound orientation
    • J. Song, Z. Zhang, W. Hu and Y. Chen: Small ubiquitinlike modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J Biol Chem, 280(48), 40122-9 (2005)
    • (2005) J Biol Chem , vol.280 , Issue.48 , pp. 40122-40129
    • Song, J.1    Zhang, Z.2    Hu, W.3    Chen, Y.4
  • 34
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73alpha by sumo-1. Two-hybrid screening with p73 identifies novel sumo-1-interacting proteins and a sumo-1 interaction motif
    • A. Minty, X. Dumont, M. Kaghad and D. Caput: Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J Biol Chem, 275(46), 36316-23 (2000)
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 35
    • 5144219680 scopus 로고    scopus 로고
    • Identification of a sumo-binding motif that recognizes sumo-modified proteins
    • J. Song, L. K. Durrin, T. A. Wilkinson, T. G. Krontiris and Y. Chen: Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. Proc Natl Acad Sci U S A, 101(40), 14373-8 (2004)
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.40 , pp. 14373-14378
    • Song, J.1    Durrin, L.K.2    Wilkinson, T.A.3    Krontiris, T.G.4    Chen, Y.5
  • 37
    • 33744940842 scopus 로고    scopus 로고
    • Specification of sumo1-and sumo2-interacting motifs
    • C. M. Hecker, M. Rabiller, K. Haglund, P. Bayer and I. Dikic: Specification of SUMO1-and SUMO2-interacting motifs. J Biol Chem, 281(23), 16117-27 (2006)
    • (2006) J Biol Chem , vol.281 , Issue.23 , pp. 16117-16127
    • Hecker, C.M.1    Rabiller, M.2    Haglund, K.3    Bayer, P.4    Dikic, I.5
  • 38
    • 34547683267 scopus 로고    scopus 로고
    • Sumo junction-what's your function? New insights through sumo-interacting motifs
    • O. Kerscher: SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Rep, 8(6), 550-5 (2007)
    • (2007) EMBO Rep , vol.8 , Issue.6 , pp. 550-555
    • Kerscher, O.1
  • 39
    • 59649087451 scopus 로고    scopus 로고
    • Phospho-regulated sumo interaction modules connect the sumo system to ck2 signaling
    • P. Stehmeier and S. Muller: Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling. Mol Cell, 33(3), 400-9 (2009)
    • (2009) Mol Cell , vol.33 , Issue.3 , pp. 400-409
    • Stehmeier, P.1    Muller, S.2
  • 40
    • 84863011993 scopus 로고    scopus 로고
    • Insights into high affinity small ubiquitin-like modifier (sumo) recognition by sumo-interacting motifs (sims) revealed by a combination of nmr and peptide array analysis
    • A. T. Namanja, Y. J. Li, Y. Su, S. Wong, J. Lu, L. T. Colson, C. Wu, S. S. Li and Y. Chen: Insights into high affinity small ubiquitin-like modifier (SUMO) recognition by SUMO-interacting motifs (SIMs) revealed by a combination of NMR and peptide array analysis. J Biol Chem, 287(5), 3231-40 (2012)
    • (2012) J Biol Chem , vol.287 , Issue.5 , pp. 3231-3240
    • Namanja, A.T.1    Li, Y.J.2    Su, Y.3    Wong, S.4    Lu, J.5    Colson, L.T.6    Wu, C.7    Li, S.S.8    Chen, Y.9
  • 43
    • 44449109533 scopus 로고    scopus 로고
    • Mechanism and consequences for paralogspecific sumoylation of ubiquitin-specific protease 25
    • E. Meulmeester, M. Kunze, H. H. Hsiao, H. Urlaub and F. Melchior: Mechanism and consequences for paralogspecific sumoylation of ubiquitin-specific protease 25. Mol Cell, 30(5), 610-9 (2008)
    • (2008) Mol Cell , vol.30 , Issue.5 , pp. 610-619
    • Meulmeester, E.1    Kunze, M.2    Hsiao, H.H.3    Urlaub, H.4    Melchior, F.5
  • 44
    • 33747373841 scopus 로고    scopus 로고
    • Involvement of sumo modification in mbd1-and mcaf1-mediated heterochromatin formation
    • Y. Uchimura, T. Ichimura, J. Uwada, T. Tachibana, S. Sugahara, M. Nakao and H. Saitoh: Involvement of SUMO modification in MBD1-and MCAF1-mediated heterochromatin formation. J Biol Chem, 281(32), 23180-90 (2006)
    • (2006) J Biol Chem , vol.281 , Issue.32 , pp. 23180-23190
    • Uchimura, Y.1    Ichimura, T.2    Uwada, J.3    Tachibana, T.4    Sugahara, S.5    Nakao, M.6    Saitoh, H.7
  • 45
    • 58149096433 scopus 로고    scopus 로고
    • Structure of the small ubiquitin-like modifier (sumo)-interacting motif of mbd1-containing chromatin-associated factor 1 bound to sumo-3
    • N. Sekiyama, T. Ikegami, T. Yamane, M. Ikeguchi, Y. Uchimura, D. Baba, M. Ariyoshi, H. Tochio, H. Saitoh and M. Shirakawa: Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3. J Biol Chem, 283(51), 35966-75 (2008)
    • (2008) J Biol Chem , vol.283 , Issue.51 , pp. 35966-35975
    • Sekiyama, N.1    Ikegami, T.2    Yamane, T.3    Ikeguchi, M.4    Uchimura, Y.5    Baba, D.6    Ariyoshi, M.7    Tochio, H.8    Saitoh, H.9    Shirakawa, M.10
  • 46
    • 57649198342 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (sumo) binding determines substrate recognition and paralog-selective sumo modification
    • J. Zhu, S. Zhu, C. M. Guzzo, N. A. Ellis, K. S. Sung, C. Y. Choi and M. J. Matunis: Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification. J Biol Chem, 283(43), 29405-15 (2008)
    • (2008) J Biol Chem , vol.283 , Issue.43 , pp. 29405-29415
    • Zhu, J.1    Zhu, S.2    Guzzo, C.M.3    Ellis, N.A.4    Sung, K.S.5    Choi, C.Y.6    Matunis, M.J.7
  • 47
    • 11444271001 scopus 로고    scopus 로고
    • Unique binding interactions among ubc9, sumo and ranbp2 reveal a mechanism for sumo paralog selection
    • M. H. Tatham, S. Kim, E. Jaffray, J. Song, Y. Chen and R. T. Hay: Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nat Struct Mol Biol, 12(1), 67-74 (2005)
    • (2005) Nat Struct Mol Biol , vol.12 , Issue.1 , pp. 67-74
    • Tatham, M.H.1    Kim, S.2    Jaffray, E.3    Song, J.4    Chen, Y.5    Hay, R.T.6
  • 48
    • 84856812305 scopus 로고    scopus 로고
    • Determinants of small ubiquitin-like modifier 1 (sumo1) protein specificity, e3 ligase, and sumo-rangap1 binding activities of nucleoporin ranbp2
    • J. R. Gareau, D. Reverter and C. D. Lima: Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2. J Biol Chem, 287(7), 4740-51 (2012
    • (2012) J Biol Chem , vol.287 , Issue.7 , pp. 4740-4751
    • Gareau, J.R.1    Reverter, D.2    Lima, C.D.3
  • 49
    • 77949329517 scopus 로고    scopus 로고
    • Kung: Kaposi's sarcoma-associated herpesvirus (kshv) encodes a sumo e3 ligase that is sim-dependent and sumo-2/3-specific
    • P. C. Chang, Y. Izumiya, C. Y. Wu, L. D. Fitzgerald, M. Campbell, T. J. Ellison, K. S. Lam, P. A. Luciw and H. J. Kung: Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific. J Biol Chem, 285(8), 5266-73 (2010)
    • (2010) J Biol Chem , vol.285 , Issue.8 , pp. 5266-5273
    • Chang, P.C.1    Izumiya, Y.2    Wu, C.Y.3    Fitzgerald, L.D.4    Campbell, M.5    Ellison, T.J.6    Lam, K.S.7    Luciw, P.A.8
  • 50
    • 61649103141 scopus 로고    scopus 로고
    • Protection from isopeptidase-mediated deconjugation regulates paralogselective sumoylation of rangap1
    • S. Zhu, J. Goeres, K. M. Sixt, M. Bekes, X. D. Zhang, G. S. Salvesen and M. J. Matunis: Protection from isopeptidase-mediated deconjugation regulates paralogselective sumoylation of RanGAP1. Mol Cell, 33(5), 570-80 (2009)
    • (2009) Mol Cell , vol.33 , Issue.5 , pp. 570-580
    • Zhu, S.1    Goeres, J.2    Sixt, K.M.3    Bekes, M.4    Zhang, X.D.5    Salvesen, G.S.6    Matunis, M.J.7
  • 52
    • 57649138450 scopus 로고    scopus 로고
    • Structure of the human senp7 catalytic domain and poly-sumo deconjugation activities for senp6 and senp7
    • C. D. Lima and D. Reverter: Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7. J Biol Chem, 283(46), 32045-55 (2008)
    • (2008) J Biol Chem , vol.283 , Issue.46 , pp. 32045-32055
    • Lima, C.D.1    Reverter, D.2
  • 53
    • 59349108844 scopus 로고    scopus 로고
    • Loss of sumo1 in mice affects rangap1 localization and formation of pml nuclear bodies, but is not lethal as it can be compensated by sumo2 or sumo3
    • E. Evdokimov, P. Sharma, S. J. Lockett, M. Lualdi and M. R. Kuehn: Loss of SUMO1 in mice affects RanGAP1 localization and formation of PML nuclear bodies, but is not lethal as it can be compensated by SUMO2 or SUMO3. J Cell Sci, 121(Pt 24), 4106-13 (2008)
    • (2008) J Cell Sci , vol.121 , Issue.PART 24 , pp. 4106-4113
    • Evdokimov, E.1    Sharma, P.2    Lockett, S.J.3    Lualdi, M.4    Kuehn, M.R.5
  • 55
    • 0032080337 scopus 로고    scopus 로고
    • Characterization of a second member of the sentrin family of ubiquitin-like proteins
    • T. Kamitani, K. Kito, H. P. Nguyen, T. Fukuda-Kamitani and E. T. Yeh: Characterization of a second member of the sentrin family of ubiquitin-like proteins. J Biol Chem, 273(18), 11349-53 (1998)
    • (1998) J Biol Chem , vol.273 , Issue.18 , pp. 11349-11353
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 57
    • 0032498541 scopus 로고    scopus 로고
    • Sumo-1 modification and its role in targeting the ran gtpaseactivating protein, rangap1, to the nuclear pore complex
    • M. J. Matunis, J. Wu and G. Blobel: SUMO-1 modification and its role in targeting the Ran GTPaseactivating protein, RanGAP1, to the nuclear pore complex. J Cell Biol, 140(3), 499-509 (1998)
    • (1998) J Cell Biol , vol.140 , Issue.3 , pp. 499-509
    • Matunis, M.J.1    Wu, J.2    Blobel, G.3
  • 58
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterization of the sumo-1 modification of rangap1 and its role in nuclear envelope association
    • R. Mahajan, L. Gerace and F. Melchior: Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J Cell Biol, 140(2), 259-70 (1998)
    • (1998) J Cell Biol , vol.140 , Issue.2 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 59
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier sumo-1 regulates the partitioning of pml within the nucleus
    • S. Muller, 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(1), 61-70 (1998)
    • (1998) Embo J , vol.17 , Issue.1 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 60
    • 0036809115 scopus 로고    scopus 로고
    • Sumo-1 modification represses sp3 transcriptional activation and modulates its subnuclear localization
    • S. Ross, J. L. Best, L. I. Zon and G. Gill: SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization. Mol Cell, 10(4), 831-42 (2002)
    • (2002) Mol Cell , vol.10 , Issue.4 , pp. 831-842
    • Ross, S.1    Best, J.L.2    Zon, L.I.3    Gill, G.4
  • 62
    • 0034700082 scopus 로고    scopus 로고
    • Posttranslational modification of tel and tel/aml1 by sumo-1 and cell-cycle-dependent assembly into nuclear bodies
    • S. R. Chakrabarti, R. Sood, S. Nandi and G. Nucifora: Posttranslational modification of TEL and TEL/AML1 by SUMO-1 and cell-cycle-dependent assembly into nuclear bodies. Proc Natl Acad Sci U S A, 97(24), 13281-5 (2000)
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.24 , pp. 13281-13285
    • Chakrabarti, S.R.1    Sood, R.2    Nandi, S.3    Nucifora, G.4
  • 64
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • T. Sternsdorf, K. Jensen, B. Reich and H. Will: The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J Biol Chem, 274(18), 12555-66 (1999)
    • (1999) J Biol Chem , vol.274 , Issue.18 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 66
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for sumo in protein quality control
    • M. H. Tatham, I. Matic, M. Mann and R. T. Hay: Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal, 4(178), rs4 (2011)
    • (2011) Sci Signal , vol.4 , Issue.178
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 67
    • 84857410438 scopus 로고    scopus 로고
    • Sumo-2/3 conjugates accumulating under heat shock or mg132 treatment result largely from new protein synthesis
    • M. Castoralova, D. Brezinova, M. Sveda, J. Lipov, T. Ruml and Z. Knejzlik: SUMO-2/3 conjugates accumulating under heat shock or MG132 treatment result largely from new protein synthesis. Biochim Biophys Acta, 1823(4), 911-9 (2012)
    • (2012) Biochim Biophys Acta , vol.1823 , Issue.4 , pp. 911-919
    • Castoralova, M.1    Brezinova, D.2    Sveda, M.3    Lipov, J.4    Ruml, T.5    Knejzlik, Z.6
  • 69
    • 36348964395 scopus 로고    scopus 로고
    • The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Y. Xie, O. Kerscher, M. B. Kroetz, H. F. McConchie, P. Sung and M. Hochstrasser: The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J Biol Chem, 282(47), 34176-84 (2007)
    • (2007) J Biol Chem , vol.282 , Issue.47 , pp. 34176-34184
    • Xie, Y.1    Kerscher, O.2    Kroetz, M.B.3    McConchie, H.F.4    Sung, P.5    Hochstrasser, M.6
  • 71
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of rnf4 family proteins in eukaryotes: Targeting a ubiquitin ligase to sumoylated proteins
    • H. Sun, J. D. Leverson and T. Hunter: Conserved function of RNF4 family proteins in eukaryotes: Targeting a ubiquitin ligase to SUMOylated proteins. Embo J, 26(18), 4102-12 (2007)
    • (2007) Embo J , vol.26 , Issue.18 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 72
    • 50649104647 scopus 로고    scopus 로고
    • Activation of the slx5-slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates
    • J. R. Mullen and S. J. Brill: Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates. J Biol Chem, 283(29), 19912-21 (2008)
    • (2008) J Biol Chem , vol.283 , Issue.29 , pp. 19912-19921
    • Mullen, J.R.1    Brill, S.J.2
  • 74
    • 63049110916 scopus 로고    scopus 로고
    • Quality control of a transcriptional regulator by sumo-targeted degradation
    • Z. Wang and G. Prelich: Quality control of a transcriptional regulator by SUMO-targeted degradation. Mol Cell Biol, 29(7), 1694-706 (2009)
    • (2009) Mol Cell Biol , vol.29 , Issue.7 , pp. 1694-1706
    • Wang, Z.1    Prelich, G.2
  • 77
    • 77951211689 scopus 로고    scopus 로고
    • Rnf4 and vhl regulate the proteasomal degradation of sumo-conjugated hypoxia-inducible factor-2alpha
    • M. van Hagen, R. M. Overmeer, S. S. Abolvardi and A. C. Vertegaal: RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2alpha. Nucleic Acids Res, 38(6), 1922-31 (2010)
    • (2010) Nucleic Acids Res , vol.38 , Issue.6 , pp. 1922-1931
    • Van Hagen, M.1    Overmeer, R.M.2    Abolvardi, S.S.3    Vertegaal, A.C.4
  • 79
    • 48749132434 scopus 로고    scopus 로고
    • Candidate genes implicated in type 1 diabetes susceptibility
    • M. Aribi: Candidate genes implicated in type 1 diabetes susceptibility. Curr Diabetes Rev, 4(2), 110-21 (2008)
    • (2008) Curr Diabetes Rev , vol.4 , Issue.2 , pp. 110-121
    • Aribi, M.1
  • 80
    • 39649117348 scopus 로고    scopus 로고
    • Sumo4 and its role in type 1 diabetes pathogenesis
    • C. Y. Wang and J. X. She: SUMO4 and its role in type 1 diabetes pathogenesis. Diabetes Metab Res Rev, 24(2), 93-102 (2008)
    • (2008) Diabetes Metab Res Rev , vol.24 , Issue.2 , pp. 93-102
    • Wang, C.Y.1    She, J.X.2
  • 82
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins pml and sp100 by pic1/sumo-1
    • T. Sternsdorf, K. Jensen and H. Will: Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J Cell Biol, 139(7), 1621-34 (1997)
    • (1997) J Cell Biol , vol.139 , Issue.7 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 83
    • 33748188499 scopus 로고    scopus 로고
    • Piasy mediates nemo sumoylation and nfkappab activation in response to genotoxic stress
    • A. M. Mabb, S. M. Wuerzberger-Davis and S. Miyamoto: PIASy mediates NEMO sumoylation and NFkappaB activation in response to genotoxic stress. Nat Cell Biol, 8(9), 986-93 (2006)
    • (2006) Nat Cell Biol , vol.8 , Issue.9 , pp. 986-993
    • Mabb, A.M.1    Wuerzberger-Davis, S.M.2    Miyamoto, S.3
  • 84
    • 33746305530 scopus 로고    scopus 로고
    • Viruses and sumoylation: Recent highlights
    • R. Boggio and S. Chiocca: Viruses and sumoylation: recent highlights. Curr Opin Microbiol, 9(4), 430-6 (2006)
    • (2006) Curr Opin Microbiol , vol.9 , Issue.4 , pp. 430-436
    • Boggio, R.1    Chiocca, S.2


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