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Volumn 4, Issue 9, 2003, Pages 690-699

Nuclear and unclear functions of sumo

Author keywords

[No Author keywords available]

Indexed keywords

SUMO PROTEIN;

EID: 0041837510     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1200     Document Type: Review
Times cited : (596)

References (128)
  • 1
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. Protein regulation by monoubiquitin. Nature Rev. Mol. Cell Biol. 2, 195-201 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 2
    • 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
  • 3
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan, R., Delphin, C., Guan, T., Gerace, L. & Melchior, F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88, 97-107 (1997).
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 4
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterizaton of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association
    • Mahajan, R., Gerace, L. & Melchior, F. Molecular characterizaton of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J. Cell Biol. 140, 259-270 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 5
    • 0032498541 scopus 로고    scopus 로고
    • SUMO-1 modification and its role in targeting the Ran GTPase-activating protein; RanGAP1, to the nuclear pore complex
    • Matunis, M. J., Wu, J. & Blobel, G. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein; RanGAP1, to the nuclear pore complex. J. Cell Biol. 140, 499-509 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 499-509
    • Matunis, M.J.1    Wu, J.2    Blobel, G.3
  • 6
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro, J. M., Rodriguez, M. S. & Hay, R. T. SUMO-1 modification of IκBα inhibits NF-κB activation. Mol. Cell 2, 233-239 (1998). The classic - and so far only - example of how sumoylation prevents proteasomal protein degradation by targeting the same acceptor lysine as ubiquitylation.
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 7
    • 0034523266 scopus 로고    scopus 로고
    • SUMO - Nonclassical ubiquitin
    • Melchior, F. SUMO - nonclassical ubiquitin. Annu. Rev. Cell Dev. Biol. 16, 591-626 (2000).
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 591-626
    • Melchior, F.1
  • 9
    • 0035969102 scopus 로고    scopus 로고
    • SUMO of branched proteins and nuclear bodies
    • Seeler, J. S. & Dejean, A. SUMO: of branched proteins and nuclear bodies. Oncogene 20, 7243-7249 (2001).
    • (2001) Oncogene , vol.20 , pp. 7243-7249
    • Seeler, J.S.1    Dejean, A.2
  • 10
    • 0032504021 scopus 로고    scopus 로고
    • Structure determination of the small ubiquitin-related modifier SUMO-1
    • Bayer, P. et al. Structure determination of the small ubiquitin-related modifier SUMO-1. J. Mol. Biol. 280, 275-286 (1998).
    • (1998) J. Mol. Biol. , vol.280 , pp. 275-286
    • Bayer, P.1
  • 11
    • 0035852990 scopus 로고    scopus 로고
    • Heteronuclear nuclear magnetic resonance assignments, structure and dynamics of SUMO-1, a human ubiquitin-like protein
    • Jin, C., Shiyanova, T., Shen, Z. & Liao, X. Heteronuclear nuclear magnetic resonance assignments, structure and dynamics of SUMO-1, a human ubiquitin-like protein. Int. J. Biol. Macromol, 28, 227-234 (2001).
    • (2001) Int. J. Biol. Macromol. , vol.28 , pp. 227-234
    • Jin, C.1    Shiyanova, T.2    Shen, Z.3    Liao, X.4
  • 12
    • 0036102289 scopus 로고    scopus 로고
    • Solution structure of a yeast ubiquitin-like protein Smt3: The role of structurally less defined sequences in protein-protein recognitions
    • Sheng, W. & Liao, X. Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions, Protein Sci. 11, 1482-1491 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 1482-1491
    • Sheng, W.1    Liao, X.2
  • 13
    • 0037470238 scopus 로고    scopus 로고
    • The SUMO protein modification system in Arabidopsis: Accumulation of SUMO1 and 2 conjugates is increased by stress
    • Kurepa, J. et al. The SUMO protein modification system in Arabidopsis: accumulation of SUMO1 and 2 conjugates is increased by stress. J. Biol. Chem. 278, 6862-6872 (2002).
    • (2002) J. Biol. Chem. , vol.278 , pp. 6862-6872
    • Kurepa, J.1
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Pichler, A., Gast, A., Seeler, J. S., Dejean, A. & Melchior, F. The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108, 109-120 (2002). This report shows that the nucleoporin RanBP2 (Nup358), which is located at the cytoplasmic filaments of the nuclear pore complex, is itself highly sumoylated (forming poly-SUMO chains) and has SUMO E3 ligase activity for the modification of the PML nuclear-body protein SP100.
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 17
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson, E. S. & Gupta, A. A. An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 106, 735-744 (2001). This report, and also reference 21, shows that Siz1, a yeast homologue of the mammalian PIAS proteins, is a SUMO E3 ligase for many cellular proteins, notably the yeast septins.
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 18
    • 0037954526 scopus 로고    scopus 로고
    • Characterization of SUMO conjugating enzyme mutants in Schizosaccharomyces pombe identifies a dominant negative allele which severely reduces SUMO conjugation
    • Ho, J. C. & Watts, F. Z. Characterization of SUMO conjugating enzyme mutants in Schizosaccharomyces pombe identifies a dominant negative allele which severely reduces SUMO conjugation. Biochem. J. 372, 97-102 (2003).
    • (2003) Biochem. J. , vol.372 , pp. 97-102
    • Ho, J.C.1    Watts, F.Z.2
  • 19
    • 0037422599 scopus 로고    scopus 로고
    • Positive and negative regulation of APP amyloidogenesis by sumoylation
    • Li, Y. et al. Positive and negative regulation of APP amyloidogenesis by sumoylation. Proc. Natl Acad. Sci. USA 100, 259-264 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 259-264
    • Li, Y.1
  • 20
    • 0035576737 scopus 로고    scopus 로고
    • A new RING for SUMO wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases
    • Jackson, P. K. A new RING for SUMO: wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases. Genes Dev. 15, 3053-3058 (2001). In this short review on the characterization of Siz/PtAS proteins as SUMO E3 ligases, the author makes a similar argument for the 'Zen' concept, using phosphorylation as an example.
    • (2001) Genes Dev. , vol.15 , pp. 3053-3058
    • Jackson, P.K.1
  • 21
    • 0035966066 scopus 로고    scopus 로고
    • Yeast Ull 1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates
    • Takahashi, Y., Kahyo, T., Toh, E. A., Yasuda, H. & Kikuchi, Y. Yeast Ull 1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates. J. Biol. Chem. 276, 48973-48977 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 48973-48977
    • Takahashi, Y.1    Kahyo, T.2    Toh, E.A.3    Yasuda, H.4    Kikuchi, Y.5
  • 22
    • 0034789730 scopus 로고    scopus 로고
    • Involvement of PIAS1 in the sumoylation of tumor suppressor p53
    • Kahyo, T., Nishida, T. & Yasuda, H. Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell 8, 713-718 (2001). The first report that extends the findings in yeast, reported in references 17 and 21, to show that the mammalian PIAS1 has SUMO E3 ligase activity for p53.
    • (2001) Mol. Cell , vol.8 , pp. 713-718
    • Kahyo, T.1    Nishida, T.2    Yasuda, H.3
  • 23
    • 0037022564 scopus 로고    scopus 로고
    • Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity
    • Schmidt, D. & Müller, S. Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity. Proc. Natl Acad. Sci. USA 99, 2872-2877 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2872-2877
    • Schmidt, D.1    Müller, S.2
  • 24
    • 0035576878 scopus 로고    scopus 로고
    • PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
    • Sachdev, S. et al, PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes Dev. 15, 3088-3103 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 3088-3103
    • Sachdev, S.1
  • 25
    • 0036291475 scopus 로고    scopus 로고
    • PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases
    • Kotaja, N., Karvonen, U., Janne, O. A. & Palvimo, J. J. PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases. Mol. Cell. Biol. 22, 5222-5234 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5222-5234
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 26
    • 0035812848 scopus 로고    scopus 로고
    • SP-RING for SUMO new functions bloom for a ubiquitin-like protein
    • Hochstrasser, M. SP-RING for SUMO: new functions bloom for a ubiquitin-like protein. Cell 107, 5-8 (2001).
    • (2001) Cell , vol.107 , pp. 5-8
    • Hochstrasser, M.1
  • 27
    • 18444370302 scopus 로고    scopus 로고
    • The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase
    • Kirsh, O. et al. The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J. 21, 2682-2691 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2682-2691
    • Kirsh, O.1
  • 29
    • 0032518581 scopus 로고    scopus 로고
    • Ubc9 and the conjugation of SUMO-1 to RanGAP1 and RanBP2
    • Saitoh, H. et al. Ubc9 and the conjugation of SUMO-1 to RanGAP1 and RanBP2. Curr. Biol. 8, 121-124 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 121-124
    • Saitoh, H.1
  • 30
    • 0037418829 scopus 로고    scopus 로고
    • The Polycomb protein Pc2 is a SUMO E3
    • Kagey, M. H., Melhuish, T. A. & Wotton, D. The Polycomb protein Pc2 is a SUMO E3. Cell 113, 127-137 (2003).
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 31
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro, C. A. & Weissman, A. M. RING finger proteins: mediators of ubiquitin ligase activity. Cell 102, 549-552 (2000).
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 32
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li, S. J. & Hochstrasser, M, A new protease required for cell-cycle progression in yeast. Nature 398, 246-251 (1999).
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 33
    • 0030728212 scopus 로고    scopus 로고
    • Ubch9 conjugates SUMO but not ubiquitin
    • Desterro, J. M., Thomson, J. & Hay, R. T. Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett. 417, 297-300 (1997).
    • (1997) FEBS Lett. , vol.417 , pp. 297-300
    • Desterro, J.M.1    Thomson, J.2    Hay, R.T.3
  • 35
    • 0036826887 scopus 로고    scopus 로고
    • PIAS1 and PIASxa function as SUMO-E3 ligases toward androgen receptor, and repress androgen receptor-dependent transcription
    • Nishida, T. & Yasuda, H. PIAS1 and PIASxa function as SUMO-E3 ligases toward androgen receptor, and repress androgen receptor-dependent transcription. J. Biol. Chem. 9, 41311-41317 (2002).
    • (2002) J. Biol. Chem. , vol.9 , pp. 41311-41317
    • Nishida, T.1    Yasuda, H.2
  • 36
  • 37
    • 0037385213 scopus 로고    scopus 로고
    • Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1
    • Hietakangas, V. et al. Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1. Mol. Cell. Biol. 23, 2953-2968 (2003). The phosphorylation of a specific serine residue of HSF1 precedes sumoylation, thereby providing an excellent example for the interplay between two types of post-translational modification in regulating the activity of a substrate.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2953-2968
    • Hietakangas, V.1
  • 38
    • 0036080376 scopus 로고    scopus 로고
    • Regulated SUMOylation and ubiquitination of DdMEK1 is required for proper chemotaxis
    • Sobko, A., Ma, H. & Firtel, R. A. Regulated SUMOylation and ubiquitination of DdMEK1 is required for proper chemotaxis. Dev. Cell 2, 745-756 (2002). This in-depth study of Mek1 signalling in the slime mold Dictyostelium provides important information on the role of sumoylation in nuclear export and on its interplay with other modifications, notably phosphorylation and ubiquitylation.
    • (2002) Dev. Cell , vol.2 , pp. 745-756
    • Sobko, A.1    Ma, H.2    Firtel, R.A.3
  • 39
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez, M. S., Dargemont, C. & Hay, R. T. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem. 276, 12654-12659 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 40
    • 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
    • Sternsdorf, T., Jensen, K., Reich, B. & Will, H. The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol. Chem. 274, 12555-12566 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 41
    • 0036300965 scopus 로고    scopus 로고
    • Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport
    • Pichler, A. & Melchior, F. Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport. Traffic 3, 381-387 (2002).
    • (2002) Traffic , vol.3 , pp. 381-387
    • Pichler, A.1    Melchior, F.2
  • 42
    • 0037147318 scopus 로고    scopus 로고
    • A lack of SUMO conjugation affects cNLS-dependent nuclear protein import in yeast
    • Stade, K. et al. A lack of SUMO conjugation affects cNLS-dependent nuclear protein import in yeast, J. Biol. Chem. 18, 49554-49561 (2002).
    • (2002) J. Biol. Chem. , vol.18 , pp. 49554-49561
    • Stade, K.1
  • 43
    • 0037128207 scopus 로고    scopus 로고
    • SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles
    • Joseph, J., Tan, S. H., Karpova, T. S., McNally, J. G. & Dasso, M. SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles. J. Cell Biol. 156, 595-602 (2002). Shows that sumoylation is required, not only for the interphasic targeting of the nuclear import factor RanGAP1 to the nuclear pores, but also for RanGAP1 targeting to kinetochores and mitotic spindles during mitosis, where it co-localizes with RanBP2.
    • (2002) J. Cell Biol. , vol.156 , pp. 595-602
    • Joseph, J.1    Tan, S.H.2    Karpova, T.S.3    McNally, J.G.4    Dasso, M.5
  • 44
    • 0035949590 scopus 로고    scopus 로고
    • SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein
    • Endter, C., Kzhyshkowska, J., Stauber, R. & Dobner, T. SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein. Proc. Natl Acad. Sci USA 98, 11312-11317 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11312-11317
    • Endter, C.1    Kzhyshkowska, J.2    Stauber, R.3    Dobner, T.4
  • 45
    • 0035799530 scopus 로고    scopus 로고
    • Functional analysis and intracellular localization of p53 modified by SUMO-1
    • Kwek, S. S., Derry, J., Tyner, A. L., Shen, Z. & Gudkov, A. V. Functional analysis and intracellular localization of p53 modified by SUMO-1. Oncogene 20, 2587-2599 (2001).
    • (2001) Oncogene , vol.20 , pp. 2587-2599
    • Kwek, S.S.1    Derry, J.2    Tyner, A.L.3    Shen, Z.4    Gudkov, A.V.5
  • 46
    • 0036809115 scopus 로고    scopus 로고
    • SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization
    • Ross, S., Best, J. L., Zon, L. I. & Gill, G. SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization, Mol. Cell 10, 831-842 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 831-842
    • Ross, S.1    Best, J.L.2    Zon, L.I.3    Gill, G.4
  • 47
    • 0036792683 scopus 로고    scopus 로고
    • Transcription factor Sp3 is silenced through SUMO modification by PIAS1
    • Sapetschnig, A. et al. Transcription factor Sp3 is silenced through SUMO modification by PIAS1. EMBO J. 21, 5206-5215 (2002). This paper and reference 46 illustrate a now almost prototypical example in which sumoylation is shown to be required for the function of a transcriptional repression domain.
    • (2002) EMBO J. , vol.21 , pp. 5206-5215
    • Sapetschnig, A.1
  • 48
    • 0035947677 scopus 로고    scopus 로고
    • SUMO-1 modification regulates the DNA-binding activity of heat shock transcription factor 2 (HSF2), a PML nuclear body associated transcription factor
    • Goodson, M. L. et al. SUMO-1 modification regulates the DNA-binding activity of heat shock transcription factor 2 (HSF2), a PML nuclear body associated transcription factor. J. Biol. Chem. 276, 18513-18518 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 18513-18518
    • Goodson, M.L.1
  • 49
    • 0035955662 scopus 로고    scopus 로고
    • Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification
    • Hong, Y. et al. Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification. J. Biol. Chem. 276, 40263-40267 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 40263-40267
    • Hong, Y.1
  • 50
    • 0034700082 scopus 로고    scopus 로고
    • Posttranslational modification of TEL and TEL/AML1 by SUMO-1 and cell-cycle-dependent assembly into nuclear bodies
    • Chakrabarti, S. R., Sood, R., Nandi, S. & Nucifora, G. Posttranslational modification of TEL and TEL/AML1 by SUMO-1 and cell-cycle-dependent assembly into nuclear bodies. Proc. Natl Acad. Sci. USA 97, 13281-13285 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13281-13285
    • Chakrabarti, S.R.1    Sood, R.2    Nandi, S.3    Nucifora, G.4
  • 51
    • 0037452964 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier conjugation regulates nuclear export of TEL, a putative tumor suppressor
    • Wood, L. D., Irvin, B. J., Nucifora, G., Luce, K. S. & Hiebert, S. W. Small ubiquitin-like modifier conjugation regulates nuclear export of TEL, a putative tumor suppressor. Proc. Natl Acad. Sci. USA 100, 3257-3262 (2003).
    • (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
  • 52
    • 0034635361 scopus 로고    scopus 로고
    • A functional interaction between dorsal and components of the Smt3 conjugation machinery
    • Bhaskar, V., Valentine, S. A. & Courey, A. J. A functional interaction between dorsal and components of the Smt3 conjugation machinery. J. Biol. Chem. 275, 4033-4040 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 4033-4040
    • Bhaskar, V.1    Valentine, S.A.2    Courey, A.J.3
  • 53
    • 0036136422 scopus 로고    scopus 로고
    • Conjugation of Smt3 to dorsal may potentiate the Drosophila immune response
    • Bhaskar, V., Smith, M. & Courey, A. J. Conjugation of Smt3 to dorsal may potentiate the Drosophila immune response. Mol. Cell Biol. 22, 492-504 (2002).
    • (2002) Mol. Cell Biol. , vol.22 , pp. 492-504
    • Bhaskar, V.1    Smith, M.2    Courey, A.J.3
  • 54
    • 0032547959 scopus 로고    scopus 로고
    • The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis
    • Epps, J. L. & Tanda, S. The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis. Curr. Biol. 8, 1277-1280 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1277-1280
    • Epps, J.L.1    Tanda, S.2
  • 55
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73α by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • Minty A., Dumont, X., Kaghad, M. & Caput, D. Covalent modification of p73α by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J. Biol. Chem. 275, 36316-36323 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 57
    • 2242438078 scopus 로고    scopus 로고
    • The aryl hydrocarbon receptor nuclear transporter is modulated by the SUMO-1 conjugating system
    • Tojo, M. et al. The aryl hydrocarbon receptor nuclear transporter is modulated by the SUMO-1 conjugating system. J. Biol. Chem. 277, 46576-46585 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 46576-46585
    • Tojo, M.1
  • 58
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka, H., Karvonen, U., Janne, O. A. & Palvimo, J. J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl Acad. Sci. USA 97, 14145-14150 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 59
    • 0036847208 scopus 로고    scopus 로고
    • SUMO-1 modification of the glucocorticoid receptor
    • Tian, S., Poukka, H., Palvimo, J. J. & Janne, O. A. SUMO-1 modification of the glucocorticoid receptor. Biochem. J. 29, 907-911 (2002).
    • (2002) Biochem. J. , vol.29 , pp. 907-911
    • Tian, S.1    Poukka, H.2    Palvimo, J.J.3    Janne, O.A.4
  • 60
    • 0037072795 scopus 로고    scopus 로고
    • The inhibitory function in human progesterone receptor N termini binds SUMO-1 protein to regulate autoinhibition and transrepression
    • Abdel-Hafiz, H., Takimoto, G. S., Tung, L. & Horwitz, K. B. The inhibitory function in human progesterone receptor N termini binds SUMO-1 protein to regulate autoinhibition and transrepression. J. Biol. Chem. 277, 33950-33956 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 33950-33956
    • Abdel-Hafiz, H.1    Takimoto, G.S.2    Tung, L.3    Horwitz, K.B.4
  • 62
    • 0037088588 scopus 로고    scopus 로고
    • Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
    • Bies, J., Markus, J. & Wolff, L. Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity. J. Biol. Chem. 277, 8999-9009 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 8999-9009
    • Bies, J.1    Markus, J.2    Wolff, L.3
  • 63
    • 0037064083 scopus 로고    scopus 로고
    • Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation
    • Kim, J., Cantwell, C. A., Johnson, P. F., Pfarr, C. M. & Williams, S. C. Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation. J. Biol. Chem. 277, 38037-38044 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 38037-38044
    • Kim, J.1    Cantwell, C.A.2    Johnson, P.F.3    Pfarr, C.M.4    Williams, S.C.5
  • 64
    • 0037930875 scopus 로고    scopus 로고
    • SREBPs are negatively regulated through SUMO-1 modification independent of the ubiquitin/26S proteasome pathway
    • Hirano, Y., Murata, S., Tanaka, K., Shimizu, M. & Sato, R. SREBPs are negatively regulated through SUMO-1 modification independent of the ubiquitin/26S proteasome pathway. J. Biol. Chem. 278, 16809-16819 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 16809-16819
    • Hirano, Y.1    Murata, S.2    Tanaka, K.3    Shimizu, M.4    Sato, R.5
  • 65
    • 0037163074 scopus 로고    scopus 로고
    • Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo
    • Boranta, J. J. & Hurst, H. C. Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. J. Biol. Chem. 277, 30798-30804 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 30798-30804
    • Boranta, J.J.1    Hurst, H.C.2
  • 66
    • 0037163859 scopus 로고    scopus 로고
    • PIAS3 induces SUMO-1 modification and transcriptional repression of IRF-1
    • Nakagawa, K. & Yokosawa, H. PIAS3 induces SUMO-1 modification and transcriptional repression of IRF-1. FEBS Lett. 530, 204-208 (2002).
    • (2002) FEBS Lett. , vol.530 , pp. 204-208
    • Nakagawa, K.1    Yokosawa, H.2
  • 67
    • 0033859780 scopus 로고    scopus 로고
    • A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy
    • Iniguez-Uuhi, J. A. & Pearce, D. A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy. Mol. Cell. Biol. 20, 6040-6050 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6040-6050
    • Iniguez-Uuhi, J.A.1    Pearce, D.2
  • 68
    • 0035799284 scopus 로고    scopus 로고
    • Cooperativity in transcriptional control
    • Courey, A. J. Cooperativity in transcriptional control. Curr. Biol. 11, R250-R252 (2001).
    • (2001) Curr. Biol. , vol.11
    • Courey, A.J.1
  • 69
    • 0037295721 scopus 로고    scopus 로고
    • Modification with SUMO
    • Verger, A., Perdomo, J. & Crossley, M. Modification with SUMO. EMBO Rep. 4, 137-142 (2003). A timely review outlining SUMO's effects on transcription.
    • (2003) EMBO Rep. , vol.4 , pp. 137-142
    • Verger, A.1    Perdomo, J.2    Crossley, M.3
  • 70
    • 0038100137 scopus 로고    scopus 로고
    • A synergy control motif within the attenuator domain of C/EBPα inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3
    • Subramanian, L., Benson, M. D. & Iniguez-Liuhi, J. A. A synergy control motif within the attenuator domain of C/EBPα inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3. J. Biol. Chem. 278, 9134-9141 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 9134-9141
    • Subramanian, L.1    Benson, M.D.2    Iniguez-Liuhi, J.A.3
  • 71
    • 0036721526 scopus 로고    scopus 로고
    • Potentiation of glucocorticoid receptor transcriptional activity by sumolation
    • Le Drean, Y., Mincheneau, N., Le Goff, P. & Michel, D. Potentiation of glucocorticoid receptor transcriptional activity by sumolation. Endocrinology 143, 3482-3489 (2002).
    • (2002) Endocrinology , vol.143 , pp. 3482-3489
    • Le Drean, Y.1    Mincheneau, N.2    Le Goff, P.3    Michel, D.4
  • 72
    • 0037119457 scopus 로고    scopus 로고
    • The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1
    • Kotaja, N., Karvonen, U., Janne, O. A. & Palvimo, J. J. The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1. J. Biol. Chem. 277, 30283-30288 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 30283-30288
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 73
    • 0038050244 scopus 로고    scopus 로고
    • The adenovirus protein Gam1 interferes with sumoylation of histone deacetylase 1
    • Colombo, R., Boggio, R., Seiser, C., Draetta, G. F & Chiocca, S. The adenovirus protein Gam1 interferes with sumoylation of histone deacetylase 1. EMBO Rep. 3, 1062-1068 (2002).
    • (2002) EMBO Rep. , vol.3 , pp. 1062-1068
    • Colombo, R.1    Boggio, R.2    Seiser, C.3    Draetta, G.F.4    Chiocca, S.5
  • 74
    • 0037189568 scopus 로고    scopus 로고
    • SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
    • David, G., Neptune, M. A. & DePinho, R. A. SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities. J. Biol. Chem. 277, 23658-23663 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 23658-23663
    • David, G.1    Neptune, M.A.2    DePinho, R.A.3
  • 75
    • 0037961625 scopus 로고    scopus 로고
    • p300 transcriptional repression is mediated by SUMO modification
    • Girdwood, D. et al. p300 transcriptional repression is mediated by SUMO modification. Mol. Cell 11, 1043-1054 (2003). The p300 protein, normally considered as a coactivator, has a repressor domain, the function of which is shown here to rely on the sumoylation-dependent recruitment of the HDAC6 histone deacetylase. Localization studies also indicate that SUMO-mediated transcriptional regulation could occur at the promoter level and not by sequestration into particular subnuclear domains.
    • (2003) Mol. Cell , vol.11 , pp. 1043-1054
    • Girdwood, D.1
  • 76
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of Stat3 signal transduction by PIAS3
    • Chung, C. D. et al. Specific inhibition of Stat3 signal transduction by PIAS3. Science 278, 1803-1805 (1997).
    • (1997) Science , vol.278 , pp. 1803-1805
    • Chung, C.D.1
  • 77
    • 0032169599 scopus 로고    scopus 로고
    • Inhibition of Stat1-mediated gene activation by PIAS1
    • Liu, B. et al. Inhibition of Stat1-mediated gene activation by PIAS1. Proc. Natl Acad. Sci. USA 95, 10626-10631 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 10626-10631
    • Liu, B.1
  • 78
    • 0034530046 scopus 로고    scopus 로고
    • ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation
    • Kotaja, N., Aittomaki, S., Silvennoinen, O., Palvimo, J. J. & Janne, O. A. ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation. Mol. Endocrinol. 14, 1986-2000 (2000).
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1986-2000
    • Kotaja, N.1    Aittomaki, S.2    Silvennoinen, O.3    Palvimo, J.J.4    Janne, O.A.5
  • 79
    • 0036789944 scopus 로고    scopus 로고
    • Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxβ
    • Tussie-Luna, M. I., Bayarsaihan, D., Seto, E., Ruddle, F. H. & Roy, A. L. Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxβ. Proc. Natl Acad. Sci. USA 99, 12807-12812 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12807-12812
    • Tussie-Luna, M.I.1    Bayarsaihan, D.2    Seto, E.3    Ruddle, F.H.4    Roy, A.L.5
  • 80
    • 0037124042 scopus 로고    scopus 로고
    • Androgen receptor-interacting protein 3 and other PIAS proteins cooperate with glucocorticoid receptor-interacting protein 1 in steroid receptor-dependent signaling
    • Kotaja, N., Vihinen, M., Palvimo, J. J. & Janne, O. A. Androgen receptor-interacting protein 3 and other PIAS proteins cooperate with glucocorticoid receptor-interacting protein 1 in steroid receptor-dependent signaling. J. Biol. Chem. 277, 17781-17788 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 17781-17788
    • Kotaja, N.1    Vihinen, M.2    Palvimo, J.J.3    Janne, O.A.4
  • 81
    • 0035813135 scopus 로고    scopus 로고
    • DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx α to the receptor
    • Takahashi, K. et al. DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx α to the receptor. J. Biol. Chem. 278, 37556-37563 (2001).
    • (2001) J. Biol. Chem. , vol.278 , pp. 37556-37563
    • Takahashi, K.1
  • 82
    • 0037041024 scopus 로고    scopus 로고
    • Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)
    • Megidish, T., Xu, J. H. & Xu, C. W. Activation of p53 by protein inhibitor of activated Stat1 (PIAS1). J. Biol. Chem. 277, 8255-8259 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 8255-8259
    • Megidish, T.1    Xu, J.H.2    Xu, C.W.3
  • 83
    • 0030824604 scopus 로고    scopus 로고
    • Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme
    • Hahn, S. L., Wasylyk, B., Criqui-Filipe, R. & Criqui, P. Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme. Oncogene 15, 1489-1495 (1997).
    • (1997) Oncogene , vol.15 , pp. 1489-1495
    • Hahn, S.L.1    Wasylyk, B.2    Criqui-Filipe, R.3    Criqui, P.4
  • 84
    • 0033594979 scopus 로고    scopus 로고
    • Modulation of TEL transcription activity by interaction with the ubiquitin-conjugating enzyme UBC9
    • Chakrabarti, S. R. et al. Modulation of TEL transcription activity by interaction with the ubiquitin-conjugating enzyme UBC9. Proc. Natl Acad. Sci. USA 96, 7467-7472 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7467-7472
    • Chakrabarti, S.R.1
  • 85
    • 0033516662 scopus 로고    scopus 로고
    • Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription
    • Poukka, H., Aamisalo, P., Karvonen, U., Palvimo, J. J. & Janne, O. A. Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription. J. Biol. Chem. 274, 19441-19446 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 19441-19446
    • Poukka, H.1    Aamisalo, P.2    Karvonen, U.3    Palvimo, J.J.4    Janne, O.A.5
  • 86
    • 0036809116 scopus 로고    scopus 로고
    • SUMO-1 protease-1 regulates gene transcription through PML
    • Best, J. L. et al. SUMO-1 protease-1 regulates gene transcription through PML. Mol. Cell 10, 843-855 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 843-855
    • Best, J.L.1
  • 87
    • 0034607653 scopus 로고    scopus 로고
    • c-Jun and p53 activity is modulated by SUMO-1 modification
    • Müller, S. et al. c-Jun and p53 activity is modulated by SUMO-1 modification. J. Biol. Chem. 275, 13321-13329 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 13321-13329
    • Müller, S.1
  • 88
    • 0034635958 scopus 로고    scopus 로고
    • SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage
    • Mao, Y., Sun, M., Desai, S. D. & Liu, L. F. SUMO-1 conjugation to topoisomerase I: a possible repair response to topoisomerase-mediated DNA damage. Proc. Natl Acad. Sci. USA 97, 4046-4051 (2000).
    • (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
  • 89
    • 0034714278 scopus 로고    scopus 로고
    • SUMO-1 conjugation to human DNA topoisomerase II isozymes
    • Mao, Y., Desai, S. D. & Liu, L. F. SUMO-1 conjugation to human DNA topoisomerase II isozymes. J. Biol. Chem. 275, 26066-26073 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26066-26073
    • Mao, Y.1    Desai, S.D.2    Liu, L.F.3
  • 90
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G L., Pyrowolakis, G. & Jentsch, S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141 (2002). Describes the serendipitous discovery that sumoylation, in targeting the same lysine residue on PCNA as mono- and poly-ubiquitylation, has a role in regulating alternative DNA-repair pathways.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 91
    • 0035050472 scopus 로고    scopus 로고
    • Functions of RecQ family helicases: Possible involvement of Bloom's and Werner's syndrome gene products in guarding genome integrity during DNA replication
    • Enomoto, T. Functions of RecQ family helicases: possible involvement of Bloom's and Werner's syndrome gene products in guarding genome integrity during DNA replication. J. Biochem. 129, 501-507 (2001).
    • (2001) J. Biochem. , vol.129 , pp. 501-507
    • Enomoto, T.1
  • 92
    • 0034647556 scopus 로고    scopus 로고
    • Covalent modification of the Werner's syndrome gene product with the ubiquitin-related protein, SUMO-1
    • Kawabe, Y. et al. Covalent modification of the Werner's syndrome gene product with the ubiquitin-related protein, SUMO-1. J. Biol. Chem. 275, 20963-20966 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 20963-20966
    • Kawabe, Y.1
  • 93
    • 0034810429 scopus 로고    scopus 로고
    • The N-terminal internal region of BLM is required for the formation of dols/rod-like structures which are associated with SUMO-1
    • Suzuki, H. et al. The N-terminal internal region of BLM is required for the formation of dols/rod-like structures which are associated with SUMO-1. Biochem. Biophys. Res. Commun. 286, 322-327 (2001).
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 322-327
    • Suzuki, H.1
  • 94
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland, U., Steinacher, R., Jiricny, J. & Schar, P. Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 21, 1456-1464 (2002). A striking demonstration of SUMO's ability to affect the activity of an enzyme, thymine DNA glycosylase, possibly by an allosteric mechanism.
    • (2002) EMBO J. , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 95
    • 0029044625 scopus 로고
    • Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C
    • Meluh, P. B. & Koshland, D. Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. Mol. Biol. Cell 6, 793-807 (1995). The demonstration that overexpression of yeast SUMO (Smt3) suppresses the phenotype of a temperature-sensitive mutation in Mif-2, the homologue of the mammalian centromere protein, CENP-C. Although unknown at the time, this is the first example of a genetic interaction between sumoylation and chromosome dynamics.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 793-807
    • Meluh, P.B.1    Koshland, D.2
  • 96
    • 0035004370 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease with a role in chromosome condensation regulation
    • Strunrikov, A. V., Aravind, L. & Koonin, E. V. Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease with a role in chromosome condensation regulation. Genetics 158, 95-107 (2001). This paper, similar to reference 95 above, shows genetic interactions between sumoylation (notably by Smt4/UIp2 and Siz1/PIAS) and the control of chromosome condensation in budding yeast.
    • (2001) Genetics , vol.158 , pp. 95-107
    • Strunrikov, A.V.1    Aravind, L.2    Koonin, E.V.3
  • 97
    • 0034993496 scopus 로고    scopus 로고
    • The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family
    • Had, K. L., Cook, K. R. & Karpen, G. H. The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family. Genes Dev. 15, 1334-1348 (2001). This work demonstrates that in flies, as in yeast, sumoylation might be important for chromosome structure, as mutation of the Drosophila PIAS homologue Suvar2-10/Zimp leads to defects in chromosome condensation and mitosis.
    • (2001) Genes Dev. , vol.15 , pp. 1334-1348
    • Had, K.L.1    Cook, K.R.2    Karpen, G.H.3
  • 98
    • 0034754698 scopus 로고    scopus 로고
    • Genes involved in sister chromatid separation and segregation in the budding yeast Saccharomyces cerevisiae
    • Biggins, S., Bhalla, N., Chang, A., Smith, D. L. & Murray, A. W. Genes involved in sister chromatid separation and segregation in the budding yeast Saccharomyces cerevisiae. Genetics 159, 453-470 (2001).
    • (2001) Genetics , vol.159 , pp. 453-470
    • Biggins, S.1    Bhalla, N.2    Chang, A.3    Smith, D.L.4    Murray, A.W.5
  • 99
    • 0033508431 scopus 로고    scopus 로고
    • Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation
    • Tanaka, K. et al. Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation. Mol. Cell. Biol. 19, 8660-8672 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8660-8672
    • Tanaka, K.1
  • 100
    • 0030842957 scopus 로고    scopus 로고
    • Characterisation of Schizosaccharomyces pombe rad31, a UBA-related gene required for DNA damage tolerance
    • Shayeghi, M., Doe, C. L., Tavassoli, M. & Watts, F. Z. Characterisation of Schizosaccharomyces pombe rad31, a UBA-related gene required for DNA damage tolerance. Nucl. Acids. Res. 25, 1162-1169 (1997).
    • (1997) Nucl. Acids. Res. , vol.25 , pp. 1162-1169
    • Shayeghi, M.1    Doe, C.L.2    Tavassoli, M.3    Watts, F.Z.4
  • 101
    • 0028898059 scopus 로고
    • The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis
    • al-Khodairy, F., Enoch, T., Hagan, I. M. & Carr, A. M. The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis. J. Cell Sci. 108, 475-486 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 475-486
    • Al-Khodairy, F.1    Enoch, T.2    Hagan, I.M.3    Carr, A.M.4
  • 102
    • 0029982968 scopus 로고    scopus 로고
    • Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes
    • Kovalenko, O. V. et al. Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. Proc. Natl Acad. Sci. USA 93, 2956-2963 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2956-2963
    • Kovalenko, O.V.1
  • 103
    • 0035060367 scopus 로고    scopus 로고
    • The Drosophila UBC9 homologue lesswright mediates the disjunction of homologues in meiosis I
    • Apionishev, S., Malhotra, D., Raghavachari, S., Tanda, S. & Rasooly, R. S. The Drosophila UBC9 homologue lesswright mediates the disjunction of homologues in meiosis I. Genes Cells 6, 215-224 (2001).
    • (2001) Genes Cells , vol.6 , pp. 215-224
    • Apionishev, S.1    Malhotra, D.2    Raghavachari, S.3    Tanda, S.4    Rasooly, R.S.5
  • 104
    • 0036291014 scopus 로고    scopus 로고
    • The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II
    • Bachant, J., Alcasabas, A., Blat, Y., Kleckner, N. & Elledge, S. J. The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II. Mol. Cell 9, 1169-1182 (2002). This recent report implicates sumoylation in sister-chromatid cohesion, so providing another example of the importance of this modification in regulating chromosome dynamics.
    • (2002) Mol. Cell , vol.9 , pp. 1169-1182
    • Bachant, J.1    Alcasabas, A.2    Blat, Y.3    Kleckner, N.4    Elledge, S.J.5
  • 105
    • 0033152703 scopus 로고    scopus 로고
    • The PML nuclear bodies: Actors or extras?
    • Seeler, J. S. & Dejean, A. The PML nuclear bodies: actors or extras? Curr. Opin. Genet. Dev. 9, 362-367 (1999).
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 362-367
    • Seeler, J.S.1    Dejean, A.2
  • 106
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
    • Ishov, A. M. et al. PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147, 221-234 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 221-234
    • Ishov, A.M.1
  • 107
    • 0343776952 scopus 로고    scopus 로고
    • Role of SUMO-1-modified PML in nuclear body formation
    • Zhong, S. et al. Role of SUMO-1-modified PML in nuclear body formation. Blood 95, 2748-2752 (2000).
    • (2000) Blood , vol.95 , pp. 2748-2752
    • Zhong, S.1
  • 108
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett, R. D. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20, 7266-7273 (2001).
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 109
    • 0034669124 scopus 로고    scopus 로고
    • Regulation of p53 activity in nuclear bodies by a specific PML isoform
    • Fogal, V. et al. Regulation of p53 activity in nuclear bodies by a specific PML isoform. EMBO J. 19, 6185-6195 (2000).
    • (2000) EMBO J. , vol.19 , pp. 6185-6195
    • Fogal, V.1
  • 110
    • 0036066181 scopus 로고    scopus 로고
    • Modification of Daxx by small ubiquitin-related modifier-1
    • Jang, M. S., Ryu, S. W. & Kim, E. Modification of Daxx by small ubiquitin-related modifier-1. Biochem. Biophys. Res. Commun. 295, 496-500 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 496-500
    • Jang, M.S.1    Ryu, S.W.2    Kim, E.3
  • 111
    • 0347790260 scopus 로고    scopus 로고
    • Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1
    • Kim, Y. H., Choi, C. Y. & Kim, Y. Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1. Proc. Natl Acad. Sci. USA 96, 12350-12355 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12350-12355
    • Kim, Y.H.1    Choi, C.Y.2    Kim, Y.3
  • 112
    • 0037330454 scopus 로고    scopus 로고
    • The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through both its kinase domain and a SUMO-1 interaction motif and alters the posttranslational modification of PML
    • Engelhardt, O. G. et al. The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through both its kinase domain and a SUMO-1 interaction motif and alters the posttranslational modification of PML. Exp. Cell Res. 283, 36-50 (2003).
    • (2003) Exp. Cell Res. , vol.283 , pp. 36-50
    • Engelhardt, O.G.1
  • 113
    • 0036646102 scopus 로고    scopus 로고
    • Deconstructing PML-induced premature senescence
    • Bischof, O. et al. Deconstructing PML-induced premature senescence, EMBO J. 21, 3358-3369 (2002). The demonstration that one specific splicing variant of the NB protein PML is sufficient to induce premature senescence when overexpressed. Interestingly, neither sumoylation of PML nor the structural integrity of the PML NBs seem necessary, thereby indicating that PML's pro-senescent activity occurs outside the PML NBs.
    • (2002) EMBO J. , vol.21 , pp. 3358-3369
    • Bischof, O.1
  • 114
    • 0035341813 scopus 로고    scopus 로고
    • p53 and PML: New partners in tumor suppression
    • Gottifredi, V. & Prives, C. p53 and PML: new partners in tumor suppression, Trends Cell Biol. 11, 184-187 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. 184-187
    • Gottifredi, V.1    Prives, C.2
  • 115
    • 0035028618 scopus 로고    scopus 로고
    • Common properties of nuclear body protein SP100 and TIF1 α chromatin factor: Role of SUMO modification
    • Seeler, J. S. et al. Common properties of nuclear body protein SP100 and TIF1 α chromatin factor: role of SUMO modification. Mol. Cell. Biol. 21, 3314-3324 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3314-3324
    • Seeler, J.S.1
  • 116
    • 0034018312 scopus 로고    scopus 로고
    • The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein
    • Li, S. J. & Hochstrasser, M. The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein. Mol. Cell. Biol. 20, 2367-2377 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2367-2377
    • Li, S.J.1    Hochstrasser, M.2
  • 117
    • 0037087504 scopus 로고    scopus 로고
    • Cell-cycle-dependent localisation of Uip1, aschizosaccharomyces pombe Pmt3 (SUMO)-specific protease
    • Taylor, D. L., Ho, J. C., Oliver, A. & Watts, F. Z. Cell-cycle-dependent localisation of Uip1, aschizosaccharomyces pombe Pmt3 (SUMO)-specific protease. J. Cell Sci. 115, 1113-1122 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 1113-1122
    • Taylor, D.L.1    Ho, J.C.2    Oliver, A.3    Watts, F.Z.4
  • 118
    • 0001720254 scopus 로고    scopus 로고
    • A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs
    • Kim, K. I. et al. A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs. J. Biol. Chem, 275, 14102-14106 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14102-14106
    • Kim, K.I.1
  • 119
    • 0033760171 scopus 로고    scopus 로고
    • A novel mammalian Smt3-specific isopeptidase 1 (SMT31P1) localized in the nucleolus at interphase
    • Nishida, T., Tanaka, H. & Yasuda, H. A novel mammalian Smt3-specific isopeptidase 1 (SMT31P1) localized in the nucleolus at interphase. Eur. J. Biochem. 267, 6423-6427 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6423-6427
    • Nishida, T.1    Tanaka, H.2    Yasuda, H.3
  • 120
    • 0034603179 scopus 로고    scopus 로고
    • Differential regulation of sentrinized proteins by a novel sentrin-specific protease
    • Gong, L., Millas, S., Maul, G. G. & Yeh, E. T. Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J. Biol. Chem. 275, 3355-3359 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.4
  • 121
    • 0037205460 scopus 로고    scopus 로고
    • Association of the human SUMO-1 protease SENP2 with the nuclear pore
    • Hang, J. & Dasso, M. Association of the human SUMO-1 protease SENP2 with the nuclear pore. J. Biol. Chem. 277, 19961-19966 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 19961-19966
    • Hang, J.1    Dasso, M.2
  • 122
    • 0036091419 scopus 로고    scopus 로고
    • Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of β-catenin
    • Kadoya, T. et al. Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of β-catenin. Mol. Cell. Biol. 22, 3803-3819 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3803-3819
    • Kadoya, T.1
  • 123
    • 0036724599 scopus 로고    scopus 로고
    • Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex
    • Zhang, H., Saitoh, H. & Matunis, M. J. Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. Mol. Cell. Biol. 22, 6498-6508 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6498-6508
    • Zhang, H.1    Saitoh, H.2    Matunis, M.J.3
  • 124
    • 0035914357 scopus 로고    scopus 로고
    • Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting β-catenin degradation
    • Nishida, T., Kaneko, F., Kitagawa, M. & Yasuda, H. Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting β-catenin degradation. J. Biol. Chem. 276, 39060-39066 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 39060-39066
    • Nishida, T.1    Kaneko, F.2    Kitagawa, M.3    Yasuda, H.4
  • 125
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: New wines in new bottles
    • Yeh, E. T., Gong, L. & Kamitani, T. Ubiquitin-like proteins: new wines in new bottles. Gene 248, 1-14 (2000).
    • (2000) Gene , vol.248 , pp. 1-14
    • Yeh, E.T.1    Gong, L.2    Kamitani, T.3
  • 126
    • 0038491277 scopus 로고    scopus 로고
    • NEDP1, a highly conserved cysteine protease that deNEDDylates Cullins
    • Mendoza, H. M. et al. NEDP1, a highly conserved cysteine protease that deNEDDylates Cullins. J. Biol. Chem. 278, 25637-25643 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 25637-25643
    • Mendoza, H.M.1
  • 127
    • 0043208977 scopus 로고    scopus 로고
    • DEN1 is a dual function protease capable of processing the C-terminus of Nedd8 deconjugating hyper-neddylated CUL1
    • Wu, K. et al. DEN1 is a dual function protease capable of processing the C-terminus of Nedd8 deconjugating hyper-neddylated CUL1. J. Biol. Chem. 278, 28882-28891 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 28882-28891
    • Wu, K.1
  • 128
    • 0037225962 scopus 로고    scopus 로고
    • Unconventional tethering of Ulp1 to the transport channel of the nuclear pore complex by karyopherins
    • Panse, V. G., Kuster, B., Gerstberger, T. & Hurt, E. Unconventional tethering of Ulp 1 to the transport channel of the nuclear pore complex by karyopherins. Nature Cell Biol. 5, 21-27 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 21-27
    • Panse, V.G.1    Kuster, B.2    Gerstberger, T.3    Hurt, E.4


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