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Volumn 13, Issue 5, 2012, Pages 467-481

SUMOylation in control of accurate chromosome segregation during mitosis

Author keywords

Centromere; Chromosome segregation; Fibrous corona; Kinetochore; Mitosis; Spindle assembly checkpoint (SAC); SUMO interacting motif (SIM); SUMOylation

Indexed keywords

BUB1 RELATED PROTEIN; CELL PROTEIN; CENTROMERE PROTEIN E; DNA TOPOISOMERASE (ATP HYDROLYSING); PROTEIN NUF2; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84866543814     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920312802430563     Document Type: Review
Times cited : (44)

References (160)
  • 1
    • 67649522162 scopus 로고    scopus 로고
    • Boveri revisited: Chromosomal instability, aneuploidy and tumorigenesis
    • Holland, A.J.; Cleveland, D.W. Boveri revisited: chromosomal instability, aneuploidy and tumorigenesis. Nat. Rev. Mol. Cell Biol., 2009, 10 (7), 478-487.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , Issue.7 , pp. 478-487
    • Holland, A.J.1    Cleveland, D.W.2
  • 2
    • 60949102816 scopus 로고    scopus 로고
    • A little CIN may cost a lot: Revisiting aneuploidy and cancer
    • Chandhok, N.S.; Pellman, D. A little CIN may cost a lot: revisiting aneuploidy and cancer. Curr. Opin. Genet. Dev., 2009, 19 (1), 74-81.
    • (2009) Curr. Opin. Genet. Dev. , vol.19 , Issue.1 , pp. 74-81
    • Chandhok, N.S.1    Pellman, D.2
  • 4
    • 79955413557 scopus 로고    scopus 로고
    • Centromeres: Unique chromatin structures that drive chromosome segregation
    • Verdaasdonk, J.S.; Bloom, K. Centromeres: unique chromatin structures that drive chromosome segregation. Nat. Rev. Mol. Cell Biol., 2011, 12 (5), 320-332.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , Issue.5 , pp. 320-332
    • Verdaasdonk, J.S.1    Bloom, K.2
  • 5
    • 37549071893 scopus 로고    scopus 로고
    • Molecular architecture of the kinetochore-microtubule interface
    • Cheeseman, I.M.; Desai, A. Molecular architecture of the kinetochore-microtubule interface. Nat. Rev. Mol. Cell Biol., 2008, 9 (1), 33-46.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , Issue.1 , pp. 33-46
    • Cheeseman, I.M.1    Desai, A.2
  • 7
    • 77955678038 scopus 로고    scopus 로고
    • Kinetochores: Orchestrating the chromosomal minuet
    • Stukenberg, P.T.; Foltz, D.R. Kinetochores: orchestrating the chromosomal minuet. Curr. Biol., 2010, 20 (12), R522-525.
    • (2010) Curr. Biol. , vol.20 , Issue.12
    • Stukenberg, P.T.1    Foltz, D.R.2
  • 8
    • 40749131181 scopus 로고    scopus 로고
    • Emerging roles of the SUMO pathway in mitosis
    • Dasso, M. Emerging roles of the SUMO pathway in mitosis. Cell Div., 2008, 3, 5.
    • (2008) Cell Div. , vol.3 , pp. 5
    • Dasso, M.1
  • 9
    • 77955759708 scopus 로고    scopus 로고
    • The fate of metaphase kinetochores is weighed in the balance of SUMOylation during S phase
    • Mukhopadhyay, D.; Dasso, M. The fate of metaphase kinetochores is weighed in the balance of SUMOylation during S phase. Cell Cycle, 2010, 9 (16), 3194-3201.
    • (2010) Cell Cycle , vol.9 , Issue.16 , pp. 3194-3201
    • Mukhopadhyay, D.1    Dasso, M.2
  • 10
    • 33846636841 scopus 로고    scopus 로고
    • The role of SUMO in chromosome segregation
    • Watts, F.Z. The role of SUMO in chromosome segregation. Chromosoma, 2007, 116 (1), 15-20.
    • (2007) Chromosoma , vol.116 , Issue.1 , pp. 15-20
    • Watts, F.Z.1
  • 11
    • 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., 1995, 6 (7), 793-807.
    • (1995) Mol. Biol. Cell. , vol.6 , Issue.7 , pp. 793-807
    • Meluh, P.B.1    Koshland, D.2
  • 12
    • 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., 1995, 108, 475-486.
    • (1995) J. Cell Sci. , vol.108 , pp. 475-486
    • Al-Khodairy, F.1    Enoch, T.2    Hagan, I.M.3    Carr, A.M.4
  • 13
    • 0028967267 scopus 로고
    • Role of a ubiquitinconjugating enzyme in degradation of S-and M-phase cyclins
    • Seufert, W.; Futcher, B.; Jentsch, S. Role of a ubiquitinconjugating enzyme in degradation of S-and M-phase cyclins. Nature, 1995, 373 (6509), 78-81.
    • (1995) Nature , vol.373 , Issue.6509 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 14
    • 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, 1999, 398 (6724), 246-251.
    • (1999) Nature , vol.398 , Issue.6724 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 15
    • 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., 2000, 20 (7), 2367-2377.
    • (2000) Mol. Cell Biol. , vol.20 , Issue.7 , pp. 2367-2377
    • Li, S.J.1    Hochstrasser, M.2
  • 16
    • 0030842957 scopus 로고    scopus 로고
    • Characterisation of Schizosaccharomyces pombe rad31, a UBArelated gene required for DNA damage tolerance
    • Shayeghi, M.; Doe, C.L.; Tavassoli, M.; Watts, F.Z. Characterisation of Schizosaccharomyces pombe rad31, a UBArelated gene required for DNA damage tolerance. Nucleic Acids Res., 1997, 25 (6), 1162-1169.
    • (1997) Nucleic Acids Res. , vol.25 , Issue.6 , pp. 1162-1169
    • Shayeghi, M.1    Doe, C.L.2    Tavassoli, M.3    Watts, F.Z.4
  • 17
    • 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, 2001, 159 (2), 453-470.
    • (2001) Genetics , vol.159 , Issue.2 , pp. 453-470
    • Biggins, S.1    Bhalla, N.2    Chang, A.3    Smith, D.L.4    Murray, A.W.5
  • 18
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E.S. Protein modification by SUMO. Annu. Rev. Biochem., 2004, 73, 355-382.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 20
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • Gill, G. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev., 2004, 18 (17), 2046-2059.
    • (2004) Genes Dev. , vol.18 , Issue.17 , pp. 2046-2059
    • Gill, G.1
  • 22
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay, R.T. SUMO: a history of modification. Mol. Cell, 2005, 18 (1), 1-12.
    • (2005) Mol. Cell , vol.18 , Issue.1 , pp. 1-12
    • Hay, R.T.1
  • 23
    • 70849129868 scopus 로고    scopus 로고
    • SUMOylation and deSUMOylation at a glance
    • Wang, Y.; Dasso, M. SUMOylation and deSUMOylation at a glance. J. Cell Sci., 2009, 122 (Pt 23), 4249-4252.
    • (2009) J. Cell Sci. , vol.122 , Issue.PART 23 , pp. 4249-4252
    • Wang, Y.1    Dasso, M.2
  • 24
    • 38549181148 scopus 로고    scopus 로고
    • Sumoylation regulates diverse biological processes
    • Zhao, J. Sumoylation regulates diverse biological processes. Cell Mol. Life Sci., 2007, 64 (23), 3017-3033.
    • (2007) Cell Mol. Life Sci. , vol.64 , Issue.23 , pp. 3017-3033
    • Zhao, J.1
  • 25
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPaseactivating 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-GTPaseactivating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol., 1996, 135 (6 Pt 1), 1457-1470.
    • (1996) J. Cell Biol. , vol.135 , Issue.6 PART 1 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 26
    • 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, 1997, 88 (1), 97-107.
    • (1997) Cell , vol.88 , Issue.1 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 27
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: The SUMO proteases
    • Mukhopadhyay, D.; Dasso, M. Modification in reverse: the SUMO proteases. Trends Biochem. Sci., 2007, 32 (6), 286-295.
    • (2007) Trends Biochem. Sci. , vol.32 , Issue.6 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 28
    • 63549129144 scopus 로고    scopus 로고
    • SUMOylation and De-SUMOylation: Wrestling with life's processes
    • Yeh, E.T. SUMOylation and De-SUMOylation: wrestling with life's processes. J. Biol. Chem., 2009, 284 (13), 8223-8227.
    • (2009) J. Biol. Chem. , vol.284 , Issue.13 , pp. 8223-8227
    • Yeh, E.T.1
  • 29
    • 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., 2000, 275 (5), 3355-3359.
    • (2000) J. Biol. Chem. , vol.275 , Issue.5 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.4
  • 30
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • Johnson, E.S.; Schwienhorst, I.; Dohmen, R.J.; Blobel, G. The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. Embo J., 1997, 16 (18), 5509-5519.
    • (1997) Embo J. , vol.16 , Issue.18 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 31
    • 0030826334 scopus 로고    scopus 로고
    • Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p
    • Johnson, E.S.; Blobel, G. Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p. J. Biol. Chem., 1997, 272 (43), 26799-26802.
    • (1997) J. Biol. Chem. , vol.272 , Issue.43 , pp. 26799-26802
    • Johnson, E.S.1    Blobel, G.2
  • 32
    • 0032512922 scopus 로고    scopus 로고
    • Modification of Ran GTPase-activating protein by the small ubiquitin-related modifier SUMO-1 requires Ubc9, an E2-type ubiquitin-conjugating enzyme homologue
    • Lee, G.W.; Melchior, F.; Matunis, M.J.; Mahajan, R.; Tian, Q.; Anderson, P. Modification of Ran GTPase-activating protein by the small ubiquitin-related modifier SUMO-1 requires Ubc9, an E2-type ubiquitin-conjugating enzyme homologue. J. Biol. Chem., 1998, 273 (11), 6503-6507.
    • (1998) J. Biol. Chem. , vol.273 , Issue.11 , pp. 6503-6507
    • Lee, G.W.1    Melchior, F.2    Matunis, M.J.3    Mahajan, R.4    Tian, Q.5    Anderson, P.6
  • 34
    • 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., 1997, 417 (3), 297-300.
    • (1997) FEBS Lett. , vol.417 , Issue.3 , pp. 297-300
    • Desterro, J.M.1    Thomson, J.2    Hay, R.T.3
  • 35
    • 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, 2001, 107 (1), 5-8.
    • (2001) Cell , vol.107 , Issue.1 , pp. 5-8
    • Hochstrasser, M.1
  • 36
    • 1542501958 scopus 로고    scopus 로고
    • SUMO: Ligases, isopeptidases and nuclear pores
    • Melchior, F.; Schergaut, M.; Pichler, A. SUMO: ligases, isopeptidases and nuclear pores. Trends Biochem. Sci., 2003, 28 (11), 612-618.
    • (2003) Trends Biochem. Sci. , vol.28 , Issue.11 , pp. 612-618
    • Melchior, F.1    Schergaut, M.2    Pichler, A.3
  • 37
    • 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, D.A.; Wang, M.; Matunis, M.J. The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J. Biol. Chem., 2001, 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
  • 38
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor, V.; Sampson, D.A.; Matunis, M.J.; Lima, C.D. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell, 2002, 108 (3), 345-356.
    • (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
  • 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., 2001, 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
  • 40
    • 77955999636 scopus 로고    scopus 로고
    • Sitespecific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif
    • Matic, I.; Schimmel, J.; Hendriks, I.A.; van Santen, M.A.; van de Rijke, F.; van Dam, H.; Gnad, F.; Mann, M.; Vertegaal, A.C. Sitespecific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol. Cell, 2010, 39 (4), 641-652.
    • (2010) Mol. Cell , vol.39 , Issue.4 , pp. 641-652
    • Matic, I.1    Schimmel, J.2    Hendriks, I.A.3    van Santen, M.A.4    van de Rijke, F.5    van Dam, H.6    Gnad, F.7    Mann, M.8    Vertegaal, A.C.9
  • 42
    • 69749124557 scopus 로고    scopus 로고
    • Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA
    • Yunus, A.A.; Lima, C.D. Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. Mol. Cell, 2009, 35 (5), 669-682.
    • (2009) Mol. Cell , vol.35 , Issue.5 , pp. 669-682
    • Yunus, A.A.1    Lima, C.D.2
  • 43
    • 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, 2001, 106 (6), 735-744.
    • (2001) Cell , vol.106 , Issue.6 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 44
    • 0035966066 scopus 로고    scopus 로고
    • Yeast Ull1/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 Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates. J. Biol. Chem., 2001, 276 (52), 48973-48977.
    • (2001) J. Biol. Chem. , vol.276 , Issue.52 , pp. 48973-48977
    • Takahashi, Y.1    Kahyo, T.2    Toh, E.A.3    Yasuda, H.4    Kikuchi, Y.5
  • 45
    • 23344442009 scopus 로고    scopus 로고
    • Human MMS21/NSE2 is a SUMO ligase required for DNA repair
    • Potts, P.R.; Yu, H. Human MMS21/NSE2 is a SUMO ligase required for DNA repair. Mol. Cell Biol., 2005, 25 (16), 7021-7032.
    • (2005) Mol. Cell Biol. , vol.25 , Issue.16 , pp. 7021-7032
    • Potts, P.R.1    Yu, H.2
  • 46
    • 16344370926 scopus 로고    scopus 로고
    • A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
    • Zhao, X.; Blobel, G. A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc. Natl. Acad. Sci. USA, 2005, 102 (13), 4777-4782.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.13 , pp. 4777-4782
    • Zhao, X.1    Blobel, G.2
  • 47
    • 33746604882 scopus 로고    scopus 로고
    • SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae
    • Cheng, C.H.; Lo, Y.H.; Liang, S.S.; Ti, S.C.; Lin, F.M.; Yeh, C.H.; Huang, H.Y.; Wang, T.F. SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae. Genes Dev., 2006, 20 (15), 2067-2081.
    • (2006) Genes Dev. , vol.20 , Issue.15 , pp. 2067-2081
    • Cheng, C.H.1    Lo, Y.H.2    Liang, S.S.3    Ti, S.C.4    Lin, F.M.5    Yeh, C.H.6    Huang, H.Y.7    Wang, T.F.8
  • 48
    • 0344874663 scopus 로고    scopus 로고
    • hZimp10 is an androgen receptor co-activator and forms a complex with SUMO-1 at replication foci
    • Sharma, M.; Li, X.; Wang, Y.; Zarnegar, M.; Huang, C.Y.; Palvimo, J.J.; Lim, B.; Sun, Z. hZimp10 is an androgen receptor co-activator and forms a complex with SUMO-1 at replication foci. Embo J., 2003, 22 (22), 6101-6114.
    • (2003) Embo J. , vol.22 , Issue.22 , pp. 6101-6114
    • Sharma, M.1    Li, X.2    Wang, Y.3    Zarnegar, M.4    Huang, C.Y.5    Palvimo, J.J.6    Lim, B.7    Sun, Z.8
  • 49
    • 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, 2002, 108 (1), 109-120.
    • (2002) Cell , vol.108 , Issue.1 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 50
    • 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, 2003, 113 (1), 127-137.
    • (2003) Cell , vol.113 , Issue.1 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 51
    • 25444462980 scopus 로고    scopus 로고
    • Regulation of MEF2 by histone deacetylase 4-and SIRT1 deacetylase-mediated lysine modifications
    • Zhao, X.; Sternsdorf, T.; Bolger, T.A.; Evans, R.M.; Yao, T.P. Regulation of MEF2 by histone deacetylase 4-and SIRT1 deacetylase-mediated lysine modifications. Mol. Cell Biol., 2005, 25 (19), 8456-8464.
    • (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
  • 52
    • 14844344773 scopus 로고    scopus 로고
    • Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors
    • Gregoire, S.; Yang, X.J. Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors. Mol. Cell Biol., 2005, 25 (6), 2273-2287.
    • (2005) Mol. Cell Biol. , vol.25 , Issue.6 , pp. 2273-2287
    • Gregoire, S.1    Yang, X.J.2
  • 54
    • 24144483441 scopus 로고    scopus 로고
    • Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo
    • Weger, S.; Hammer, E.; Heilbronn, R. Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo. FEBS Lett., 2005, 579 (22), 5007-5012.
    • (2005) FEBS Lett. , vol.579 , Issue.22 , pp. 5007-5012
    • Weger, S.1    Hammer, E.2    Heilbronn, R.3
  • 55
    • 36048929872 scopus 로고    scopus 로고
    • The E3 ligase Topors induces the accumulation of polysumoylated forms of DNA topoisomerase I in vitro and in vivo
    • Hammer, E.; Heilbronn, R.; Weger, S. The E3 ligase Topors induces the accumulation of polysumoylated forms of DNA topoisomerase I in vitro and in vivo. FEBS Lett., 2007, 581 (28), 5418-5424.
    • (2007) FEBS Lett. , vol.581 , Issue.28 , pp. 5418-5424
    • Hammer, E.1    Heilbronn, R.2    Weger, S.3
  • 57
    • 34548483908 scopus 로고    scopus 로고
    • SUMO-specific proteases: A twist in the tail
    • Hay, R.T. SUMO-specific proteases: a twist in the tail. Trends Cell Biol., 2007, 17 (8), 370-376.
    • (2007) Trends Cell Biol. , vol.17 , Issue.8 , pp. 370-376
    • Hay, R.T.1
  • 58
    • 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 Ulp1 to the transport channel of the nuclear pore complex by karyopherins. Nat. Cell Biol., 2003, 5 (1), 21-27.
    • (2003) Nat. Cell Biol. , vol.5 , Issue.1 , pp. 21-27
    • Panse, V.G.1    Kuster, B.2    Gerstberger, T.3    Hurt, E.4
  • 60
    • 33748574525 scopus 로고    scopus 로고
    • Formation and nuclear export of preribosomes are functionally linked to the small-ubiquitin-related modifier pathway
    • Panse, V.G.; Kressler, D.; Pauli, A.; Petfalski, E.; Gnadig, M.; Tollervey, D.; Hurt, E. Formation and nuclear export of preribosomes are functionally linked to the small-ubiquitin-related modifier pathway. Traffic, 2006, 7 (10), 1311-1321.
    • (2006) Traffic , vol.7 , Issue.10 , pp. 1311-1321
    • Panse, V.G.1    Kressler, D.2    Pauli, A.3    Petfalski, E.4    Gnadig, M.5    Tollervey, D.6    Hurt, E.7
  • 61
    • 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, 2002, 9 (6), 1169-1182.
    • (2002) Mol. Cell , vol.9 , Issue.6 , pp. 1169-1182
    • Bachant, J.1    Alcasabas, A.2    Blat, Y.3    Kleckner, N.4    Elledge, S.J.5
  • 62
    • 0242414786 scopus 로고    scopus 로고
    • The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast
    • Bylebyl, G.R.; Belichenko, I.; Johnson, E.S. The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast. J. Biol. Chem., 2003, 278 (45), 44113-44120.
    • (2003) J. Biol. Chem. , vol.278 , Issue.45 , pp. 44113-44120
    • Bylebyl, G.R.1    Belichenko, I.2    Johnson, E.S.3
  • 63
    • 0037417333 scopus 로고    scopus 로고
    • The Ulp1 SUMO isopeptidase: Distinct domains required for viability, nuclear envelope localization, and substrate specificity
    • Li, S.J.; Hochstrasser, M. The Ulp1 SUMO isopeptidase: distinct domains required for viability, nuclear envelope localization, and substrate specificity. J. Cell Biol., 2003, 160 (7), 1069-1081.
    • (2003) J. Cell Biol. , vol.160 , Issue.7 , pp. 1069-1081
    • Li, S.J.1    Hochstrasser, M.2
  • 64
    • 4143083663 scopus 로고    scopus 로고
    • A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
    • Reverter, D.; Lima, C.D. A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. Structure, 2004, 12 (8), 1519-1531.
    • (2004) Structure , vol.12 , Issue.8 , pp. 1519-1531
    • Reverter, D.1    Lima, C.D.2
  • 65
    • 33746038148 scopus 로고    scopus 로고
    • The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing
    • Shen, L.N.; Dong, C.; Liu, H.; Naismith, J.H.; Hay, R.T. The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem. J., 2006, 397 (2), 279-288.
    • (2006) Biochem. J. , vol.397 , Issue.2 , pp. 279-288
    • Shen, L.N.1    Dong, C.2    Liu, H.3    Naismith, J.H.4    Hay, R.T.5
  • 66
    • 14844299866 scopus 로고    scopus 로고
    • Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1
    • Xu, Z.; Au, S.W. Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. Biochem. J., 2005, 386 (Pt 2), 325-330.
    • (2005) Biochem. J. , vol.386 , Issue.PART 2 , pp. 325-330
    • Xu, Z.1    Au, S.W.2
  • 67
    • 0346422441 scopus 로고    scopus 로고
    • Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1
    • Bailey, D.; O'Hare, P. Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1. J. Biol. Chem., 2004, 279 (1), 692-703.
    • (2004) J. Biol. Chem. , vol.279 , Issue.1 , pp. 692-703
    • Bailey, D.1    O'Hare, P.2
  • 68
    • 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., 2002, 277 (22), 19961-19966.
    • (2002) J. Biol. Chem. , vol.277 , Issue.22 , pp. 19961-19966
    • Hang, J.1    Dasso, M.2
  • 69
    • 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., 2002, 22 (18), 6498-6508.
    • (2002) Mol. Cell Biol. , vol.22 , Issue.18 , pp. 6498-6508
    • Zhang, H.1    Saitoh, H.2    Matunis, M.J.3
  • 70
    • 84055176117 scopus 로고    scopus 로고
    • The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex
    • Goeres, J.; Chan, P.K.; Mukhopadhyay, D.; Zhang, H.; Raught, B.; Matunis, M.J. The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex. Mol. Biol. Cell, 2011, 22 (24), 4868-4882.
    • (2011) Mol. Biol. Cell , vol.22 , Issue.24 , pp. 4868-4882
    • Goeres, J.1    Chan, P.K.2    Mukhopadhyay, D.3    Zhang, H.4    Raught, B.5    Matunis, M.J.6
  • 71
    • 33745049415 scopus 로고    scopus 로고
    • The SUMO-specific protease SENP5 is required for cell division
    • Di Bacco, A.; Ouyang, J.; Lee, H.Y.; Catic, A.; Ploegh, H.; Gill, G. The SUMO-specific protease SENP5 is required for cell division. Mol. Cell Biol., 2006, 26 (12), 4489-4498.
    • (2006) Mol. Cell Biol. , vol.26 , Issue.12 , pp. 4489-4498
    • Di Bacco, A.1    Ouyang, J.2    Lee, H.Y.3    Catic, A.4    Ploegh, H.5    Gill, G.6
  • 72
    • 33744917849 scopus 로고    scopus 로고
    • Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3
    • Gong, L.; Yeh, E.T. Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3. J. Biol. Chem., 2006, 281 (23), 15869-15877.
    • (2006) J. Biol. Chem. , vol.281 , Issue.23 , pp. 15869-15877
    • Gong, L.1    Yeh, E.T.2
  • 73
    • 58149195377 scopus 로고    scopus 로고
    • Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases
    • Yun, C.; Wang, Y.; Mukhopadhyay, D.; Backlund, P.; Kolli, N.; Yergey, A.; Wilkinson, K.D.; Dasso, M. Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases. J. Cell Biol., 2008, 183 (4), 589-595.
    • (2008) J. Cell Biol. , vol.183 , Issue.4 , pp. 589-595
    • Yun, C.1    Wang, Y.2    Mukhopadhyay, D.3    Backlund, P.4    Kolli, N.5    Yergey, A.6    Wilkinson, K.D.7    Dasso, M.8
  • 74
    • 57649138450 scopus 로고    scopus 로고
    • Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7
    • Lima, C.D.; Reverter, D. Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7. J. Biol. Chem., 2008, 283 (46), 32045-32055.
    • (2008) J. Biol. Chem. , vol.283 , Issue.46 , pp. 32045-32055
    • Lima, C.D.1    Reverter, D.2
  • 76
    • 40849115019 scopus 로고    scopus 로고
    • SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis
    • Zhang, X.D.; Goeres, J.; Zhang, H.; Yen, T.J.; Porter, A.C.; Matunis, M.J. SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. Mol. Cell, 2008, 29 (6), 729-741.
    • (2008) Mol. Cell , vol.29 , Issue.6 , pp. 729-741
    • Zhang, X.D.1    Goeres, J.2    Zhang, H.3    Yen, T.J.4    Porter, A.C.5    Matunis, M.J.6
  • 77
    • 21844437072 scopus 로고    scopus 로고
    • PIASy mediates SUMO-2 conjugation of Topoisomerase-II on mitotic chromosomes
    • Azuma, Y.; Arnaoutov, A.; Anan, T.; Dasso, M. PIASy mediates SUMO-2 conjugation of Topoisomerase-II on mitotic chromosomes. Embo J., 2005, 24 (12), 2172-2182.
    • (2005) Embo J. , vol.24 , Issue.12 , pp. 2172-2182
    • Azuma, Y.1    Arnaoutov, A.2    Anan, T.3    Dasso, M.4
  • 78
    • 67650115041 scopus 로고    scopus 로고
    • Genetic and proteomic evidence for roles of Drosophila SUMO in cell cycle control, Ras signaling, and early pattern formation
    • Nie, M.; Xie, Y.; Loo, J.A.; Courey, A.J. Genetic and proteomic evidence for roles of Drosophila SUMO in cell cycle control, Ras signaling, and early pattern formation. PLoS ONE, 2009, 4 (6), e5905.
    • (2009) PLoS ONE , vol.4 , Issue.6
    • Nie, M.1    Xie, Y.2    Loo, J.A.3    Courey, A.J.4
  • 79
    • 77954056702 scopus 로고    scopus 로고
    • Contrasting models for kinetochore microtubule attachment in mammalian cells
    • McEwen, B.F.; Dong, Y. Contrasting models for kinetochore microtubule attachment in mammalian cells. Cell Mol. Life Sci., 2010, 67 (13), 2163-2172.
    • (2010) Cell Mol. Life Sci. , vol.67 , Issue.13 , pp. 2163-2172
    • McEwen, B.F.1    Dong, Y.2
  • 80
    • 0037459109 scopus 로고    scopus 로고
    • Centromeres and kinetochores: From epigenetics to mitotic checkpoint signaling
    • Cleveland, D.W.; Mao, Y.; Sullivan, K.F. Centromeres and kinetochores: from epigenetics to mitotic checkpoint signaling. Cell, 2003, 112 (4), 407-421.
    • (2003) Cell , vol.112 , Issue.4 , pp. 407-421
    • Cleveland, D.W.1    Mao, Y.2    Sullivan, K.F.3
  • 81
    • 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., 2002, 156 (4), 595-602.
    • (2002) J. Cell Biol. , vol.156 , Issue.4 , pp. 595-602
    • Joseph, J.1    Tan, S.H.2    Karpova, T.S.3    McNally, J.G.4    Dasso, M.5
  • 82
    • 0242509262 scopus 로고    scopus 로고
    • SUMO-2/3 regulates topoisomerase II in mitosis
    • Azuma, Y.; Arnaoutov, A.; Dasso, M. SUMO-2/3 regulates topoisomerase II in mitosis. J. Cell Biol., 2003, 163 (3), 477-487.
    • (2003) J. Cell Biol. , vol.163 , Issue.3 , pp. 477-487
    • Azuma, Y.1    Arnaoutov, A.2    Dasso, M.3
  • 83
    • 0035883939 scopus 로고    scopus 로고
    • Creation and characterization of temperature-sensitive CENP-C mutants in vertebrate cells
    • Fukagawa, T.; Regnier, V.; Ikemura, T. Creation and characterization of temperature-sensitive CENP-C mutants in vertebrate cells. Nucleic Acids Res., 2001, 29 (18), 3796-3803.
    • (2001) Nucleic Acids Res. , vol.29 , Issue.18 , pp. 3796-3803
    • Fukagawa, T.1    Regnier, V.2    Ikemura, T.3
  • 84
    • 79956311920 scopus 로고    scopus 로고
    • Mitotic kinase Aurora-B is regulated by SUMO-2/3 conjugation/deconjugation during mitosis
    • Ban, R.; Nishida, T.; Urano, T. Mitotic kinase Aurora-B is regulated by SUMO-2/3 conjugation/deconjugation during mitosis. Genes Cells, 2011, 16 (6), 652-669.
    • (2011) Genes Cells , vol.16 , Issue.6 , pp. 652-669
    • Ban, R.1    Nishida, T.2    Urano, T.3
  • 86
    • 63049102038 scopus 로고    scopus 로고
    • RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin
    • Klein, U.R.; Haindl, M.; Nigg, E.A.; Muller, S. RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin. Mol. Biol. Cell, 2009, 20 (1), 410-418.
    • (2009) Mol. Biol. Cell , vol.20 , Issue.1 , pp. 410-418
    • Klein, U.R.1    Haindl, M.2    Nigg, E.A.3    Muller, S.4
  • 87
    • 78349263872 scopus 로고    scopus 로고
    • PIASy-dependent SUMOylation regulates DNA topoisomerase IIalpha activity
    • Ryu, H.; Furuta, M.; Kirkpatrick, D.; Gygi, S.P.; Azuma, Y. PIASy-dependent SUMOylation regulates DNA topoisomerase IIalpha activity. J. Cell Biol., 2010, 191 (4), 783-794.
    • (2010) J. Cell Biol. , vol.191 , Issue.4 , pp. 783-794
    • Ryu, H.1    Furuta, M.2    Kirkpatrick, D.3    Gygi, S.P.4    Azuma, Y.5
  • 88
    • 77949378117 scopus 로고    scopus 로고
    • The SUMO protease SENP6 is essential for inner kinetochore assembly
    • Mukhopadhyay, D.; Arnaoutov, A.; Dasso, M. The SUMO protease SENP6 is essential for inner kinetochore assembly. J. Cell Biol., 2010, 188 (5), 681-692.
    • (2010) J. Cell Biol. , vol.188 , Issue.5 , pp. 681-692
    • Mukhopadhyay, D.1    Arnaoutov, A.2    Dasso, M.3
  • 90
    • 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., 1998, 140 (3), 499-509.
    • (1998) J. Cell Biol. , vol.140 , Issue.3 , pp. 499-509
    • Matunis, M.J.1    Wu, J.2    Blobel, G.3
  • 91
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association
    • Mahajan, R.; Gerace, L.; Melchior, F. Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J. Cell Biol., 1998, 140 (2), 259-270.
    • (1998) J. Cell Biol. , vol.140 , Issue.2 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 92
    • 1842715846 scopus 로고    scopus 로고
    • The RanGAP1-RanBP2 complex is essential for microtubulekinetochore interactions in vivo
    • Joseph, J.; Liu, S.T.; Jablonski, S.A.; Yen, T.J.; Dasso, M. The RanGAP1-RanBP2 complex is essential for microtubulekinetochore interactions in vivo. Curr. Biol., 2004, 14 (7), 611-617.
    • (2004) Curr. Biol. , vol.14 , Issue.7 , pp. 611-617
    • Joseph, J.1    Liu, S.T.2    Jablonski, S.A.3    Yen, T.J.4    Dasso, M.5
  • 94
    • 0037043338 scopus 로고    scopus 로고
    • Rapid exchange of mammalian topoisomerase II alpha at kinetochores and chromosome arms in mitosis
    • Tavormina, P.A.; Come, M.G.; Hudson, J.R.; Mo, Y.Y.; Beck, W.T.; Gorbsky, G.J. Rapid exchange of mammalian topoisomerase II alpha at kinetochores and chromosome arms in mitosis. J. Cell Biol., 2002, 158 (1), 23-29.
    • (2002) J. Cell Biol. , vol.158 , Issue.1 , pp. 23-29
    • Tavormina, P.A.1    Come, M.G.2    Hudson, J.R.3    Mo, Y.Y.4    Beck, W.T.5    Gorbsky, G.J.6
  • 95
    • 63049138013 scopus 로고    scopus 로고
    • SUMO modification of DNA topoisomerase II: Trying to get a CENse of it all
    • Lee, M.T.; Bachant, J. SUMO modification of DNA topoisomerase II: trying to get a CENse of it all. DNA Repair (Amst), 2009, 8 (4), 557-568.
    • (2009) DNA Repair (Amst) , vol.8 , Issue.4 , pp. 557-568
    • Lee, M.T.1    Bachant, J.2
  • 96
    • 34247333444 scopus 로고    scopus 로고
    • The spindle-assembly checkpoint in space and time
    • Musacchio, A.; Salmon, E.D. The spindle-assembly checkpoint in space and time. Nat. Rev. Mol. Cell Biol., 2007, 8 (5), 379-393.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , Issue.5 , pp. 379-393
    • Musacchio, A.1    Salmon, E.D.2
  • 97
    • 67649484355 scopus 로고    scopus 로고
    • Clearing the way for mitosis: Is cohesin a target?
    • Yanagida, M. Clearing the way for mitosis: is cohesin a target? Nat. Rev. Mol. Cell Biol., 2009, 10 (7), 489-496.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , Issue.7 , pp. 489-496
    • Yanagida, M.1
  • 98
    • 13544254815 scopus 로고    scopus 로고
    • Topoisomerase II: Untangling its contribution at the centromere
    • Porter, A.C.; Farr, C.J. Topoisomerase II: untangling its contribution at the centromere. Chromosome Res., 2004, 12 (6), 569-583.
    • (2004) Chromosome Res. , vol.12 , Issue.6 , pp. 569-583
    • Porter, A.C.1    Farr, C.J.2
  • 99
    • 33644761942 scopus 로고    scopus 로고
    • SIZ1/SIZ2 control of chromosome transmission fidelity is mediated by the sumoylation of topoisomerase II
    • Takahashi, Y.; Yong-Gonzalez, V.; Kikuchi, Y.; Strunnikov, A. SIZ1/SIZ2 control of chromosome transmission fidelity is mediated by the sumoylation of topoisomerase II. Genetics, 2006, 172 (2), 783-794.
    • (2006) Genetics , vol.172 , Issue.2 , pp. 783-794
    • Takahashi, Y.1    Yong-Gonzalez, V.2    Kikuchi, Y.3    Strunnikov, A.4
  • 100
    • 42049102803 scopus 로고    scopus 로고
    • Conjugation of human topoisomerase 2 alpha with small ubiquitinlike modifiers 2/3 in response to topoisomerase inhibitors: Cell cycle stage and chromosome domain specificity
    • Agostinho, M.; Santos, V.; Ferreira, F.; Costa, R.; Cardoso, J.; Pinheiro, I.; Rino, J.; Jaffray, E.; Hay, R.T.; Ferreira, J. Conjugation of human topoisomerase 2 alpha with small ubiquitinlike modifiers 2/3 in response to topoisomerase inhibitors: cell cycle stage and chromosome domain specificity. Cancer Res., 2008, 68 (7), 2409-2418.
    • (2008) Cancer Res. , vol.68 , Issue.7 , pp. 2409-2418
    • Agostinho, M.1    Santos, V.2    Ferreira, F.3    Costa, R.4    Cardoso, J.5    Pinheiro, I.6    Rino, J.7    Jaffray, E.8    Hay, R.T.9    Ferreira, J.10
  • 103
    • 77957770103 scopus 로고    scopus 로고
    • Rod/Zw10 complex is required for PIASydependent centromeric SUMOylation
    • Ryu, H.; Azuma, Y. Rod/Zw10 complex is required for PIASydependent centromeric SUMOylation. J. Biol. Chem., 2010, 285 (42), 32576-32585.
    • (2010) J. Biol. Chem. , vol.285 , Issue.42 , pp. 32576-32585
    • Ryu, H.1    Azuma, Y.2
  • 104
  • 105
    • 0242551545 scopus 로고    scopus 로고
    • The cellular geography of aurora kinases
    • Carmena, M.; Earnshaw, W.C. The cellular geography of aurora kinases. Nat. Rev. Mol. Cell Biol., 2003, 4 (11), 842-854.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , Issue.11 , pp. 842-854
    • Carmena, M.1    Earnshaw, W.C.2
  • 106
    • 33751227843 scopus 로고    scopus 로고
    • Kinetochore microtubule dynamics and attachment stability are regulated by Hec1
    • DeLuca, J.G.; Gall, W.E.; Ciferri, C.; Cimini, D.; Musacchio, A.; Salmon, E.D. Kinetochore microtubule dynamics and attachment stability are regulated by Hec1. Cell, 2006, 127 (5), 969-982.
    • (2006) Cell , vol.127 , Issue.5 , pp. 969-982
    • DeLuca, J.G.1    Gall, W.E.2    Ciferri, C.3    Cimini, D.4    Musacchio, A.5    Salmon, E.D.6
  • 107
    • 33748112986 scopus 로고    scopus 로고
    • Sumoylation of the budding yeast kinetochore protein Ndc10 is required for Ndc10 spindle localization and regulation of anaphase spindle elongation
    • Montpetit, B.; Hazbun, T.R.; Fields, S.; Hieter, P. Sumoylation of the budding yeast kinetochore protein Ndc10 is required for Ndc10 spindle localization and regulation of anaphase spindle elongation. J. Cell Biol., 2006, 174 (5), 653-663.
    • (2006) J. Cell Biol. , vol.174 , Issue.5 , pp. 653-663
    • Montpetit, B.1    Hazbun, T.R.2    Fields, S.3    Hieter, P.4
  • 108
    • 80054114082 scopus 로고    scopus 로고
    • The ABCs of CENPs
    • Perpelescu, M.; Fukagawa, T. The ABCs of CENPs. Chromosoma, 2011, 120 (5), 425-446.
    • (2011) Chromosoma , vol.120 , Issue.5 , pp. 425-446
    • Perpelescu, M.1    Fukagawa, T.2
  • 109
    • 33744970012 scopus 로고    scopus 로고
    • The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres
    • Okada, M.; Cheeseman, I.M.; Hori, T.; Okawa, K.; McLeod, I.X.; Yates, J.R., 3rd; Desai, A.; Fukagawa, T. The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres. Nat. Cell Biol., 2006, 8 (5), 446-457.
    • (2006) Nat. Cell Biol. , vol.8 , Issue.5 , pp. 446-457
    • Okada, M.1    Cheeseman, I.M.2    Hori, T.3    Okawa, K.4    McLeod, I.X.5    Yates 3rd, J.R.6    Desai, A.7    Fukagawa, T.8
  • 110
    • 39449096363 scopus 로고    scopus 로고
    • KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly in vertebrates
    • Cheeseman, I.M.; Hori, T.; Fukagawa, T.; Desai, A. KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly in vertebrates. Mol. Biol. Cell, 2008, 19 (2), 587-594.
    • (2008) Mol. Biol. Cell , vol.19 , Issue.2 , pp. 587-594
    • Cheeseman, I.M.1    Hori, T.2    Fukagawa, T.3    Desai, A.4
  • 111
    • 33751232957 scopus 로고    scopus 로고
    • The conserved KMN network constitutes the core microtubulebinding site of the kinetochore
    • Cheeseman, I.M.; Chappie, J.S.; Wilson-Kubalek, E.M.; Desai, A. The conserved KMN network constitutes the core microtubulebinding site of the kinetochore. Cell, 2006, 127 (5), 983-997.
    • (2006) Cell , vol.127 , Issue.5 , pp. 983-997
    • Cheeseman, I.M.1    Chappie, J.S.2    Wilson-Kubalek, E.M.3    Desai, A.4
  • 113
    • 33750463100 scopus 로고    scopus 로고
    • SUMO: The glue that binds
    • Matunis, M.J.; Zhang, X.D.; Ellis, N.A. SUMO: the glue that binds. Dev. Cell, 2006, 11 (5), 596-597.
    • (2006) Dev. Cell , vol.11 , Issue.5 , pp. 596-597
    • Matunis, M.J.1    Zhang, X.D.2    Ellis, N.A.3
  • 114
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function? New insights through SUMO-interacting motifs
    • Kerscher, O. SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Rep., 2007, 8 (6), 550-555.
    • (2007) EMBO Rep. , vol.8 , Issue.6 , pp. 550-555
    • Kerscher, O.1
  • 115
    • 4544386818 scopus 로고    scopus 로고
    • In vitro modification of human centromere protein CENP-C fragments by small ubiquitin-like modifier (SUMO) protein: Definitive identification of the modification sites by tandem mass spectrometry analysis of the isopeptides
    • Chung, T.L.; Hsiao, H.H.; Yeh, Y.Y.; Shia, H.L.; Chen, Y.L.; Liang, P.H.; Wang, A.H.; Khoo, K.H.; Shoei-Lung Li, S. In vitro modification of human centromere protein CENP-C fragments by small ubiquitin-like modifier (SUMO) protein: definitive identification of the modification sites by tandem mass spectrometry analysis of the isopeptides. J. Biol. Chem., 2004, 279 (38), 39653-39662.
    • (2004) J. Biol. Chem. , vol.279 , Issue.38 , pp. 39653-39662
    • Chung, T.L.1    Hsiao, H.H.2    Yeh, Y.Y.3    Shia, H.L.4    Chen, Y.L.5    Liang, P.H.6    Wang, A.H.7    Khoo, K.H.8    Shoei-Lung Li, S.9
  • 116
    • 76649092335 scopus 로고    scopus 로고
    • Soluble cytoplasmic expression, rapid purification, and characterization of cyanovirin-N as a His-SUMO fusion
    • Gao, X.; Chen, W.; Guo, C.; Qian, C.; Liu, G.; Ge, F.; Huang, Y.; Kitazato, K.; Wang, Y.; Xiong, S. Soluble cytoplasmic expression, rapid purification, and characterization of cyanovirin-N as a His-SUMO fusion. Appl. Microbiol. Biotechnol., 2009, 85 (4), 1051-1060.
    • (2009) Appl. Microbiol. Biotechnol. , vol.85 , Issue.4 , pp. 1051-1060
    • Gao, X.1    Chen, W.2    Guo, C.3    Qian, C.4    Liu, G.5    Ge, F.6    Huang, Y.7    Kitazato, K.8    Wang, Y.9    Xiong, S.10
  • 117
    • 50049088245 scopus 로고    scopus 로고
    • Enhanced protein expression in mammalian cells using engineered SUMO fusions: Secreted phospholipase A2
    • Peroutka, R.J.; Elshourbagy, N.; Piech, T.; Butt, T.R. Enhanced protein expression in mammalian cells using engineered SUMO fusions: secreted phospholipase A2. Protein Sci., 2008, 17 (9), 1586-1595.
    • (2008) Protein Sci. , vol.17 , Issue.9 , pp. 1586-1595
    • Peroutka, R.J.1    Elshourbagy, N.2    Piech, T.3    Butt, T.R.4
  • 118
    • 53149112694 scopus 로고    scopus 로고
    • Enhanced protein expression in the baculovirus/insect cell system using engineered SUMO fusions
    • Liu, L.; Spurrier, J.; Butt, T.R.; Strickler, J.E. Enhanced protein expression in the baculovirus/insect cell system using engineered SUMO fusions. Protein Expr. Purif., 2008, 62 (1), 21-28.
    • (2008) Protein Expr. Purif. , vol.62 , Issue.1 , pp. 21-28
    • Liu, L.1    Spurrier, J.2    Butt, T.R.3    Strickler, J.E.4
  • 119
    • 34247324364 scopus 로고    scopus 로고
    • Systematic analysis of fusion and affinity tags using human aspartyl-tRNA synthetase expressed in E. coli
    • Guzzo, C.M.; Yang, D.C. Systematic analysis of fusion and affinity tags using human aspartyl-tRNA synthetase expressed in E. coli. Protein Expr. Purif., 2007, 54 (1), 166-175.
    • (2007) Protein Expr. Purif. , vol.54 , Issue.1 , pp. 166-175
    • Guzzo, C.M.1    Yang, D.C.2
  • 120
    • 29344475982 scopus 로고    scopus 로고
    • Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO
    • Marblestone, J.G.; Edavettal, S.C.; Lim, Y.; Lim, P.; Zuo, X.; Butt, T.R. Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO. Protein Sci., 2006, 15 (1), 182-189.
    • (2006) Protein Sci. , vol.15 , Issue.1 , pp. 182-189
    • Marblestone, J.G.1    Edavettal, S.C.2    Lim, Y.3    Lim, P.4    Zuo, X.5    Butt, T.R.6
  • 121
    • 34547101028 scopus 로고    scopus 로고
    • Human NUF2 interacts with centromere-associated protein E and is essential for a stable spindle microtubule-kinetochore attachment
    • Liu, D.; Ding, X.; Du, J.; Cai, X.; Huang, Y.; Ward, T.; Shaw, A.; Yang, Y.; Hu, R.; Jin, C.; Yao, X. Human NUF2 interacts with centromere-associated protein E and is essential for a stable spindle microtubule-kinetochore attachment. J. Biol. Chem., 2007, 282 (29), 21415-21424.
    • (2007) J. Biol. Chem. , vol.282 , Issue.29 , pp. 21415-21424
    • Liu, D.1    Ding, X.2    Du, J.3    Cai, X.4    Huang, Y.5    Ward, T.6    Shaw, A.7    Yang, Y.8    Hu, R.9    Jin, C.10    Yao, X.11
  • 122
    • 0001665802 scopus 로고    scopus 로고
    • CENP-E forms a link between attachment of spindle microtubules to kinetochores and the mitotic checkpoint
    • Yao, X.; Abrieu, A.; Zheng, Y.; Sullivan, K.F.; Cleveland, D.W. CENP-E forms a link between attachment of spindle microtubules to kinetochores and the mitotic checkpoint. Nat. Cell Biol., 2000, 2 (8), 484-491.
    • (2000) Nat. Cell Biol. , vol.2 , Issue.8 , pp. 484-491
    • Yao, X.1    Abrieu, A.2    Zheng, Y.3    Sullivan, K.F.4    Cleveland, D.W.5
  • 123
    • 0032487444 scopus 로고    scopus 로고
    • Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1
    • Chan, G.K.; Schaar, B.T.; Yen, T.J. Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1. J. Cell Biol., 1998, 143 (1), 49-63.
    • (1998) J. Cell Biol. , vol.143 , Issue.1 , pp. 49-63
    • Chan, G.K.1    Schaar, B.T.2    Yen, T.J.3
  • 124
    • 79958748578 scopus 로고    scopus 로고
    • The Ndc80 complex: Integrating the kinetochore's many movements
    • Tooley, J.; Stukenberg, P.T. The Ndc80 complex: integrating the kinetochore's many movements. Chromosome Res., 2011, 19 (3), 377-391.
    • (2011) Chromosome Res. , vol.19 , Issue.3 , pp. 377-391
    • Tooley, J.1    Stukenberg, P.T.2
  • 125
    • 34250006846 scopus 로고    scopus 로고
    • The Ndc80 complex: Hub of kinetochore activity
    • Ciferri, C.; Musacchio, A.; Petrovic, A. The Ndc80 complex: hub of kinetochore activity. FEBS Lett., 2007, 581 (15), 2862-2869.
    • (2007) FEBS Lett. , vol.581 , Issue.15 , pp. 2862-2869
    • Ciferri, C.1    Musacchio, A.2    Petrovic, A.3
  • 126
    • 61649103141 scopus 로고    scopus 로고
    • Protection from isopeptidase-mediated deconjugation regulates paralog-selective sumoylation of RanGAP1
    • Zhu, S.; Goeres, J.; Sixt, K.M.; Bekes, M.; Zhang, X.D.; Salvesen, G.S.; Matunis, M.J. Protection from isopeptidase-mediated deconjugation regulates paralog-selective sumoylation of RanGAP1. Mol. Cell, 2009, 33 (5), 570-580.
    • (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
  • 127
    • 0036744787 scopus 로고    scopus 로고
    • Unstable kinetochoremicrotubule capture and chromosomal instability following deletion of CENP-E
    • Putkey, F.R.; Cramer, T.; Morphew, M.K.; Silk, A.D.; Johnson, R.S.; McIntosh, J.R.; Cleveland, D.W. Unstable kinetochoremicrotubule capture and chromosomal instability following deletion of CENP-E. Dev. Cell, 2002, 3 (3), 351-365.
    • (2002) Dev. Cell , vol.3 , Issue.3 , pp. 351-365
    • Putkey, F.R.1    Cramer, T.2    Morphew, M.K.3    Silk, A.D.4    Johnson, R.S.5    McIntosh, J.R.6    Cleveland, D.W.7
  • 128
    • 0030665077 scopus 로고    scopus 로고
    • CENP-E is a plus end-directed kinetochore motor required for metaphase chromosome alignment
    • Wood, K.W.; Sakowicz, R.; Goldstein, L.S.; Cleveland, D.W. CENP-E is a plus end-directed kinetochore motor required for metaphase chromosome alignment. Cell, 1997, 91 (3), 357-366.
    • (1997) Cell , vol.91 , Issue.3 , pp. 357-366
    • Wood, K.W.1    Sakowicz, R.2    Goldstein, L.S.3    Cleveland, D.W.4
  • 129
    • 0034631826 scopus 로고    scopus 로고
    • CENP-meta, an essential kinetochore kinesin required for the maintenance of metaphase chromosome alignment in Drosophila
    • Yucel, J.K.; Marszalek, J.D.; McIntosh, J.R.; Goldstein, L.S.; Cleveland, D.W.; Philp, A.V. CENP-meta, an essential kinetochore kinesin required for the maintenance of metaphase chromosome alignment in Drosophila. J. Cell Biol., 2000, 150 (1), 1-11.
    • (2000) J. Cell Biol. , vol.150 , Issue.1 , pp. 1-11
    • Yucel, J.K.1    Marszalek, J.D.2    McIntosh, J.R.3    Goldstein, L.S.4    Cleveland, D.W.5    Philp, A.V.6
  • 131
    • 43149106486 scopus 로고    scopus 로고
    • CENP-E combines a slow, processive motor and a flexible coiled coil to produce an essential motile kinetochore tether
    • Kim, Y.; Heuser, J.E.; Waterman, C.M.; Cleveland, D.W. CENP-E combines a slow, processive motor and a flexible coiled coil to produce an essential motile kinetochore tether. J. Cell Biol., 2008, 181 (3), 411-419.
    • (2008) J. Cell Biol. , vol.181 , Issue.3 , pp. 411-419
    • Kim, Y.1    Heuser, J.E.2    Waterman, C.M.3    Cleveland, D.W.4
  • 132
    • 0031468113 scopus 로고    scopus 로고
    • CENP-E function at kinetochores is essential for chromosome alignment
    • Schaar, B.T.; Chan, G.K.; Maddox, P.; Salmon, E.D.; Yen, T.J. CENP-E function at kinetochores is essential for chromosome alignment. J. Cell Biol., 1997, 139 (6), 1373-1382.
    • (1997) J. Cell Biol. , vol.139 , Issue.6 , pp. 1373-1382
    • Schaar, B.T.1    Chan, G.K.2    Maddox, P.3    Salmon, E.D.4    Yen, T.J.5
  • 136
    • 0030963425 scopus 로고    scopus 로고
    • RanBP2 associates with Ubc9p and a modified form of RanGAP1
    • Saitoh, H.; Pu, R.; Cavenagh, M.; Dasso, M. RanBP2 associates with Ubc9p and a modified form of RanGAP1. Proc. Natl. Acad. Sci. USA, 1997, 94 (8), 3736-3741.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.8 , pp. 3736-3741
    • Saitoh, H.1    Pu, R.2    Cavenagh, M.3    Dasso, M.4
  • 137
    • 20444384040 scopus 로고    scopus 로고
    • Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
    • Reverter, D.; Lima, C.D. Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature, 2005, 435 (7042), 687-692.
    • (2005) Nature , vol.435 , Issue.7042 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 138
    • 46249113438 scopus 로고    scopus 로고
    • The RanGTP gradient-a GPS for the mitotic spindle
    • Kalab, P.; Heald, R. The RanGTP gradient-a GPS for the mitotic spindle. J. Cell Sci., 2008, 121 (Pt 10), 1577-1586.
    • (2008) J. Cell Sci. , vol.121 , Issue.PART 10 , pp. 1577-1586
    • Kalab, P.1    Heald, R.2
  • 139
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • table of contents
    • Macara, I.G. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev., 2001, 65 (4), 570-594, table of contents.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , Issue.4 , pp. 570-594
    • Macara, I.G.1
  • 142
    • 0141545024 scopus 로고    scopus 로고
    • Nup358 integrates nuclear envelope breakdown with kinetochore assembly
    • Salina, D.; Enarson, P.; Rattner, J.B.; Burke, B. Nup358 integrates nuclear envelope breakdown with kinetochore assembly. J. Cell Biol., 2003, 162 (6), 991-1001.
    • (2003) J. Cell Biol. , vol.162 , Issue.6 , pp. 991-1001
    • Salina, D.1    Enarson, P.2    Rattner, J.B.3    Burke, B.4
  • 143
    • 35548986309 scopus 로고    scopus 로고
    • Regulation of cell cycle progression and gene expression by H2A deubiquitination
    • Joo, H.Y.; Zhai, L.; Yang, C.; Nie, S.; Erdjument-Bromage, H.; Tempst, P.; Chang, C.; Wang, H. Regulation of cell cycle progression and gene expression by H2A deubiquitination. Nature, 2007, 449 (7165), 1068-1072.
    • (2007) Nature , vol.449 , Issue.7165 , pp. 1068-1072
    • Joo, H.Y.1    Zhai, L.2    Yang, C.3    Nie, S.4    Erdjument-Bromage, H.5    Tempst, P.6    Chang, C.7    Wang, H.8
  • 146
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for SUMO in protein quality control
    • Tatham, M.H.; Matic, I.; Mann, M.; Hay, R.T. Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci. Signal, 2011, 4 (178), rs4.
    • (2011) Sci. Signal , vol.4 , Issue.178
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 147
    • 28544453333 scopus 로고    scopus 로고
    • Chromosome alignment and segregation regulated by ubiquitination of survivin
    • Vong, Q.P.; Cao, K.; Li, H.Y.; Iglesias, P.A.; Zheng, Y. Chromosome alignment and segregation regulated by ubiquitination of survivin. Science, 2005, 310 (5753), 1499-1504.
    • (2005) Science , vol.310 , Issue.5753 , pp. 1499-1504
    • Vong, Q.P.1    Cao, K.2    Li, H.Y.3    Iglesias, P.A.4    Zheng, Y.5
  • 148
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart, C.M.; Fushman, D. Polyubiquitin chains: polymeric protein signals. Curr. Opin. Chem. Biol., 2004, 8 (6), 610-616.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , Issue.6 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 149
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • Desterro, J.M.; Rodriguez, M.S.; Hay, R.T. SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol. Cell, 1998, 2 (2), 233-239.
    • (1998) Mol. Cell , vol.2 , Issue.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 150
    • 25844437172 scopus 로고    scopus 로고
    • Mutual interactions between the SUMO and ubiquitin systems: A plea of no contest
    • Ulrich, H.D. Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest. Trends Cell Biol., 2005, 15 (10), 525-532.
    • (2005) Trends Cell Biol. , vol.15 , Issue.10 , pp. 525-532
    • Ulrich, H.D.1
  • 151
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan, G.L.; Pfander, B.; Jentsch, S. PCNA, the maestro of the replication fork. Cell, 2007, 129 (4), 665-679.
    • (2007) Cell , vol.129 , Issue.4 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 152
    • 0035921418 scopus 로고    scopus 로고
    • Elevating the level of Cdc34/Ubc3 ubiquitin-conjugating enzyme in mitosis inhibits association of CENP-E with kinetochores and blocks the metaphase alignment of chromosomes
    • Topper, L.M.; Bastians, H.; Ruderman, J.V.; Gorbsky, G.J. Elevating the level of Cdc34/Ubc3 ubiquitin-conjugating enzyme in mitosis inhibits association of CENP-E with kinetochores and blocks the metaphase alignment of chromosomes. J. Cell Biol., 2001, 154 (4), 707-717.
    • (2001) J. Cell Biol. , vol.154 , Issue.4 , pp. 707-717
    • Topper, L.M.1    Bastians, H.2    Ruderman, J.V.3    Gorbsky, G.J.4
  • 153
    • 0025782910 scopus 로고
    • CENP-E, a novel human centromere-associated protein required for progression from metaphase to anaphase
    • Yen, T.J.; Compton, D.A.; Wise, D.; Zinkowski, R.P.; Brinkley, B.R.; Earnshaw, W.C.; Cleveland, D.W. CENP-E, a novel human centromere-associated protein required for progression from metaphase to anaphase. Embo J., 1991, 10 (5), 1245-1254.
    • (1991) Embo J. , vol.10 , Issue.5 , pp. 1245-1254
    • Yen, T.J.1    Compton, D.A.2    Wise, D.3    Zinkowski, R.P.4    Brinkley, B.R.5    Earnshaw, W.C.6    Cleveland, D.W.7
  • 154
    • 0029903059 scopus 로고    scopus 로고
    • The kinesin-like protein CENP-E is kinetochore-associated throughout poleward chromosome segregation during anaphase-A
    • Brown, K.D.; Wood, K.W.; Cleveland, D.W. The kinesin-like protein CENP-E is kinetochore-associated throughout poleward chromosome segregation during anaphase-A. J. Cell Sci., 1996, 109 (Pt 5), 961-969.
    • (1996) J. Cell Sci. , vol.109 , Issue.PART 5 , pp. 961-969
    • Brown, K.D.1    Wood, K.W.2    Cleveland, D.W.3
  • 155
    • 2342439525 scopus 로고    scopus 로고
    • Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression
    • Johnson, V.L.; Scott, M.I.; Holt, S.V.; Hussein, D.; Taylor, S.S. Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression. J. Cell Sci., 2004, 117 (Pt 8), 1577-1589.
    • (2004) J. Cell Sci. , vol.117 , Issue.PART 8 , pp. 1577-1589
    • Johnson, V.L.1    Scott, M.I.2    Holt, S.V.3    Hussein, D.4    Taylor, S.S.5
  • 156
    • 69249209892 scopus 로고    scopus 로고
    • Defects in chromosome congression and mitotic progression in KIF18Adeficient cells are partly mediated through impaired functions of CENP-E
    • Huang, Y.; Yao, Y.; Xu, H.Z.; Wang, Z.G.; Lu, L.; Dai, W. Defects in chromosome congression and mitotic progression in KIF18Adeficient cells are partly mediated through impaired functions of CENP-E. Cell Cycle, 2009, 8 (16), 2643-2649.
    • (2009) Cell Cycle , vol.8 , Issue.16 , pp. 2643-2649
    • Huang, Y.1    Yao, Y.2    Xu, H.Z.3    Wang, Z.G.4    Lu, L.5    Dai, W.6
  • 157
    • 77954043950 scopus 로고    scopus 로고
    • Nuclear transport and the mitotic apparatus: An evolving relationship
    • Wozniak, R.; Burke, B.; Doye, V. Nuclear transport and the mitotic apparatus: an evolving relationship. Cell Mol. Life Sci., 67 (13), 2215-2230.
    • Cell Mol. Life Sci. , vol.67 , Issue.13 , pp. 2215-2230
    • Wozniak, R.1    Burke, B.2    Doye, V.3
  • 158
    • 18844449387 scopus 로고    scopus 로고
    • Recruitment of Mad2 to the kinetochore requires the Rod/Zw10 complex
    • Buffin, E.; Lefebvre, C.; Huang, J.; Gagou, M.E.; Karess, R.E. Recruitment of Mad2 to the kinetochore requires the Rod/Zw10 complex. Curr. Biol., 2005, 15 (9), 856-861.
    • (2005) Curr. Biol. , vol.15 , Issue.9 , pp. 856-861
    • Buffin, E.1    Lefebvre, C.2    Huang, J.3    Gagou, M.E.4    Karess, R.E.5
  • 159
    • 0037694976 scopus 로고    scopus 로고
    • Zwilch, a new component of the ZW10/ROD complex required for kinetochore functions
    • Williams, B.C.; Li, Z.; Liu, S.; Williams, E.V.; Leung, G.; Yen, T.J.; Goldberg, M.L. Zwilch, a new component of the ZW10/ROD complex required for kinetochore functions. Mol. Biol. Cell, 2003, 14 (4), 1379-1391.
    • (2003) Mol. Biol. Cell , vol.14 , Issue.4 , pp. 1379-1391
    • Williams, B.C.1    Li, Z.2    Liu, S.3    Williams, E.V.4    Leung, G.5    Yen, T.J.6    Goldberg, M.L.7
  • 160
    • 21744436611 scopus 로고    scopus 로고
    • Rod-Zw10-Zwilch: A key player in the spindle checkpoint
    • Karess, R. Rod-Zw10-Zwilch: a key player in the spindle checkpoint. Trends Cell Biol., 2005, 15 (7), 386-392.
    • (2005) Trends Cell Biol. , vol.15 , Issue.7 , pp. 386-392
    • Karess, R.1


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