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Volumn 288, Issue 38, 2013, Pages 27085-27099

O-linked N-acetylglucosamine cycling regulates mitotic spindle organization

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; PROTEINS;

EID: 84884550720     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.470187     Document Type: Article
Times cited : (28)

References (51)
  • 1
    • 79955413557 scopus 로고    scopus 로고
    • Centromeres: Unique chromatin structures that drive chromosome segregation
    • Verdaasdonk, J. S., and Bloom, K. (2011) Centromeres: unique chromatin structures that drive chromosome segregation. Nat. Rev. Mol. Cell Biol. 12, 320-332
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 320-332
    • Verdaasdonk, J.S.1    Bloom, K.2
  • 3
    • 84869115074 scopus 로고    scopus 로고
    • Microtubule assembly during mitosis - From distinct origins to distinct functions?
    • Meunier, S., and Vernos, I. (2012) Microtubule assembly during mitosis - from distinct origins to distinct functions? J. Cell Sci. 125, 2805-2814
    • (2012) J. Cell Sci. , vol.125 , pp. 2805-2814
    • Meunier, S.1    Vernos, I.2
  • 4
    • 1642289364 scopus 로고    scopus 로고
    • Linked for life: Temporal and spatial coordination of late mitotic events
    • Seshan, A., and Amon, A. (2004) Linked for life: temporal and spatial coordination of late mitotic events. Curr. Opin. Cell Biol. 16, 41-48
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 41-48
    • Seshan, A.1    Amon, A.2
  • 5
    • 84861880210 scopus 로고    scopus 로고
    • Chromosomal instability and aneuploidy in cancer: From yeast to man
    • Pfau, S. J., and Amon, A. (2012) Chromosomal instability and aneuploidy in cancer: from yeast to man. EMBO Rep. 13, 515-527
    • (2012) EMBO Rep. , vol.13 , pp. 515-527
    • Pfau, S.J.1    Amon, A.2
  • 6
    • 10744225982 scopus 로고    scopus 로고
    • CENP-A phosphorylation by Aurora-A in prophase is required for enrichment of Aurora-B at inner centromeres and for kinetochore function
    • Kunitoku, N., Sasayama, T., Marumoto, T., Zhang, D., Honda, S., Kobayashi, O., Hatakeyama, K., Ushio, Y., Saya, H., and Hirota, T. (2003) CENP-A phosphorylation by Aurora-A in prophase is required for enrichment of Aurora-B at inner centromeres and for kinetochore function. Dev. Cell 5, 853-864
    • (2003) Dev. Cell , vol.5 , pp. 853-864
    • Kunitoku, N.1    Sasayama, T.2    Marumoto, T.3    Zhang, D.4    Honda, S.5    Kobayashi, O.6    Hatakeyama, K.7    Ushio, Y.8    Saya, H.9    Hirota, T.10
  • 7
    • 0035235736 scopus 로고    scopus 로고
    • Mitotic kinases as regulators of cell division and its checkpoints
    • Nigg, E. A. (2001) Mitotic kinases as regulators of cell division and its checkpoints. Nat. Rev. Mol. Cell Biol. 2, 21-32
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 21-32
    • Nigg, E.A.1
  • 10
    • 77951952612 scopus 로고    scopus 로고
    • Aurora B phosphorylates spatially distinct targets to differentially regulate the kinetochore-microtubule interface
    • Welburn, J. P., Vleugel, M., Liu, D., Yates, J. R., 3rd, Lampson, M. A., Fukagawa, T., and Cheeseman, I. M. (2010) Aurora B phosphorylates spatially distinct targets to differentially regulate the kinetochore-microtubule interface. Mol. Cell 38, 383-392
    • (2010) Mol. Cell , vol.38 , pp. 383-392
    • Welburn, J.P.1    Vleugel, M.2    Liu, D.3    Yates III, J.R.4    Lampson, M.A.5    Fukagawa, T.6    Cheeseman, I.M.7
  • 11
    • 77955928431 scopus 로고    scopus 로고
    • Dual detection of chromosomes and microtubules by the chromosomal passenger complex drives spindle assembly
    • Tseng, B. S., Tan, L., Kapoor, T. M., and Funabiki, H. (2010) Dual detection of chromosomes and microtubules by the chromosomal passenger complex drives spindle assembly. Dev. Cell 18, 903-912
    • (2010) Dev. Cell , vol.18 , pp. 903-912
    • Tseng, B.S.1    Tan, L.2    Kapoor, T.M.3    Funabiki, H.4
  • 12
    • 0036732808 scopus 로고    scopus 로고
    • Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation
    • Bolton, M. A., Lan, W., Powers, S. E., McCleland, M. L., Kuang, J., and Stukenberg, P. T. (2002) Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation. Mol. Biol. Cell 13, 3064-3077
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3064-3077
    • Bolton, M.A.1    Lan, W.2    Powers, S.E.3    McCleland, M.L.4    Kuang, J.5    Stukenberg, P.T.6
  • 15
    • 34249327737 scopus 로고    scopus 로고
    • Phosphorylation and activation of cell division cycle associated 8 by aurora kinase B plays a significant role in human lung carcinogenesis
    • Hayama, S., Daigo, Y., Yamabuki, T., Hirata, D., Kato, T., Miyamoto, M., Ito, T., Tsuchiya, E., Kondo, S., and Nakamura, Y. (2007) Phosphorylation and activation of cell division cycle associated 8 by aurora kinase B plays a significant role in human lung carcinogenesis. Cancer Res. 67, 4113-4122
    • (2007) Cancer Res. , vol.67 , pp. 4113-4122
    • Hayama, S.1    Daigo, Y.2    Yamabuki, T.3    Hirata, D.4    Kato, T.5    Miyamoto, M.6    Ito, T.7    Tsuchiya, E.8    Kondo, S.9    Nakamura, Y.10
  • 16
    • 25444501339 scopus 로고    scopus 로고
    • Perturbations in O-linkedα-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis
    • Slawson, C., Zachara, N. E., Vosseller, K., Cheung, W. D., Lane, M. D., and Hart, G. W. (2005) Perturbations in O-linkedα-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis. J. Biol. Chem. 280, 32944-32956
    • (2005) J. Biol. Chem. , vol.280 , pp. 32944-32956
    • Slawson, C.1    Zachara, N.E.2    Vosseller, K.3    Cheung, W.D.4    Lane, M.D.5    Hart, G.W.6
  • 17
    • 57349187712 scopus 로고    scopus 로고
    • A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin
    • Slawson, C., Lakshmanan, T., Knapp, S., and Hart, G. W. (2008) A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin. Mol. Biol. Cell 19, 4130-4140
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4130-4140
    • Slawson, C.1    Lakshmanan, T.2    Knapp, S.3    Hart, G.W.4
  • 18
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: Implications for cancer cell biology
    • Slawson, C., and Hart, G. W. (2011) O-GlcNAc signalling: implications for cancer cell biology. Nat. Rev. Cancer 11, 678-684
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 20
    • 78049390185 scopus 로고    scopus 로고
    • O-GlcNAc transferase regulates mitotic chromatin dynamics
    • Sakabe, K., and Hart, G. W. (2010) O-GlcNAc transferase regulates mitotic chromatin dynamics. J. Biol. Chem. 285, 34460-34468
    • (2010) J. Biol. Chem. , vol.285 , pp. 34460-34468
    • Sakabe, K.1    Hart, G.W.2
  • 21
    • 0242582455 scopus 로고    scopus 로고
    • Diabetes and the accompanying hyperglycemia impairs cardiomyocyte calcium cycling through increased nuclear O-GlcNAcylation
    • Clark, R. J., McDonough, P. M., Swanson, E., Trost, S. U., Suzuki, M., Fukuda, M., and Dillmann, W. H. (2003) Diabetes and the accompanying hyperglycemia impairs cardiomyocyte calcium cycling through increased nuclear O-GlcNAcylation. J. Biol. Chem. 278, 44230-44237
    • (2003) J. Biol. Chem. , vol.278 , pp. 44230-44237
    • Clark, R.J.1    McDonough, P.M.2    Swanson, E.3    Trost, S.U.4    Suzuki, M.5    Fukuda, M.6    Dillmann, W.H.7
  • 23
    • 78650447665 scopus 로고    scopus 로고
    • α-N-acetylglucosamine (O-GlcNAc) is part of the histone code
    • Sakabe, K., Wang, Z., and Hart, G. W. (2010) α-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc. Natl. Acad. Sci. U. S. A. 107, 19915-19920
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 19915-19920
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 25
    • 84861211043 scopus 로고    scopus 로고
    • TPPP acts downstream of RhoA-ROCK-LIMK2 to regulate astral microtubule organization and spindle orientation
    • Heng, Y. W., Lim, H. H., Mina, T., Utomo, P., Zhong, S., Lim, C. T., and Koh, C. G. (2012) TPPP acts downstream of RhoA-ROCK-LIMK2 to regulate astral microtubule organization and spindle orientation. J. Cell Sci. 125, 1579-1590
    • (2012) J. Cell Sci. , vol.125 , pp. 1579-1590
    • Heng, Y.W.1    Lim, H.H.2    Mina, T.3    Utomo, P.4    Zhong, S.5    Lim, C.T.6    Koh, C.G.7
  • 26
    • 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., and Salmon, E. D. (2006) Kinetochore microtubule dynamics and attachment stability are regulated by Hec1. Cell 127, 969-982
    • (2006) Cell , vol.127 , pp. 969-982
    • De Luca, J.G.1    Gall, W.E.2    Ciferri, C.3    Cimini, D.4    Musacchio, A.5    Salmon, E.D.6
  • 27
    • 44849107340 scopus 로고    scopus 로고
    • Mitotic CDKs control the metaphaseanaphase transition and trigger spindle elongation
    • Rahal, R., and Amon, A. (2008) Mitotic CDKs control the metaphaseanaphase transition and trigger spindle elongation. Genes Dev. 22, 1534-1548
    • (2008) Genes Dev. , vol.22 , pp. 1534-1548
    • Rahal, R.1    Amon, A.2
  • 31
    • 0037446847 scopus 로고    scopus 로고
    • A novel mechanism for activation of the protein kinase Aurora A
    • Eyers, P. A., Erikson, E., Chen, L. G., and Maller, J. L. (2003) A novel mechanism for activation of the protein kinase Aurora A. Curr. Biol. 13, 691-697
    • (2003) Curr. Biol. , vol.13 , pp. 691-697
    • Eyers, P.A.1    Erikson, E.2    Chen, L.G.3    Maller, J.L.4
  • 32
    • 0141429171 scopus 로고    scopus 로고
    • Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells
    • Hirota, T., Kunitoku, N., Sasayama, T., Marumoto, T., Zhang, D., Nitta, M., Hatakeyama, K., and Saya, H. (2003) Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells. Cell 114, 585-598
    • (2003) Cell , vol.114 , pp. 585-598
    • Hirota, T.1    Kunitoku, N.2    Sasayama, T.3    Marumoto, T.4    Zhang, D.5    Nitta, M.6    Hatakeyama, K.7    Saya, H.8
  • 33
    • 0034609753 scopus 로고    scopus 로고
    • The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation
    • Walter, A. O., Seghezzi, W., Korver, W., Sheung, J., and Lees, E. (2000) The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation. Oncogene 19, 4906-4916
    • (2000) Oncogene , vol.19 , pp. 4906-4916
    • Walter, A.O.1    Seghezzi, W.2    Korver, W.3    Sheung, J.4    Lees, E.5
  • 34
    • 54549100243 scopus 로고    scopus 로고
    • Pituitary tumor transforming gene 1 regulates Aurora kinase A activity
    • Tong, Y., Ben-Shlomo, A., Zhou, C., Wawrowsky, K., and Melmed, S. (2008) Pituitary tumor transforming gene 1 regulates Aurora kinase A activity. Oncogene 27, 6385-6395
    • (2008) Oncogene , vol.27 , pp. 6385-6395
    • Tong, Y.1    Ben-Shlomo, A.2    Zhou, C.3    Wawrowsky, K.4    Melmed, S.5
  • 35
    • 0037113919 scopus 로고    scopus 로고
    • Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase
    • Jang, Y. J., Ma, S., Terada, Y., and Erikson, R. L. (2002) Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase. J. Biol. Chem. 277, 44115-44120
    • (2002) J. Biol. Chem. , vol.277 , pp. 44115-44120
    • Jang, Y.J.1    Ma, S.2    Terada, Y.3    Erikson, R.L.4
  • 36
    • 58249085900 scopus 로고    scopus 로고
    • The catalytic role of INCENP in Aurora B activation and the kinetic mechanism of Aurora B/INCENP
    • Yang, J., Zappacosta, F., Annan, R. S., Nurse, K., Tummino, P. J., Copeland, R. A., and Lai, Z. (2009) The catalytic role of INCENP in Aurora B activation and the kinetic mechanism of Aurora B/INCENP. Biochem. J. 417, 355-360
    • (2009) Biochem. J. , vol.417 , pp. 355-360
    • Yang, J.1    Zappacosta, F.2    Annan, R.S.3    Nurse, K.4    Tummino, P.J.5    Copeland, R.A.6    Lai, Z.7
  • 37
    • 0035945340 scopus 로고    scopus 로고
    • CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis
    • Zeitlin, S. G., Shelby, R. D., and Sullivan, K. F. (2001) CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis. J. Cell Biol. 155, 1147-1157
    • (2001) J. Cell Biol. , vol.155 , pp. 1147-1157
    • Zeitlin, S.G.1    Shelby, R.D.2    Sullivan, K.F.3
  • 38
    • 0035911159 scopus 로고    scopus 로고
    • Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytoki-nesis
    • Giet, R., and Glover, D. M. (2001) Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytoki-nesis. J. Cell Biol. 152, 669-682
    • (2001) J. Cell Biol. , vol.152 , pp. 669-682
    • Giet, R.1    Glover, D.M.2
  • 39
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei, Y., Yu, L., Bowen, J., Gorovsky, M. A., and Allis, C. D. (1999) Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 97, 99-109
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 40
    • 80054818714 scopus 로고    scopus 로고
    • Modification of histones by sugar α-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated
    • Zhang, S., Roche, K., Nasheuer, H. P., and Lowndes, N. F. (2011) Modification of histones by sugar α-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated. J. Biol. Chem. 286, 37483-37495
    • (2011) J. Biol. Chem. , vol.286 , pp. 37483-37495
    • Zhang, S.1    Roche, K.2    Nasheuer, H.P.3    Lowndes, N.F.4
  • 41
    • 84859512121 scopus 로고    scopus 로고
    • α-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3
    • Fong, J. J., Nguyen, B. L., Bridger, R., Medrano, E. E., Wells, L., Pan, S., and Sifers, R. N. (2012) α-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3. J. Biol. Chem. 287, 12195-12203
    • (2012) J. Biol. Chem. , vol.287 , pp. 12195-12203
    • Fong, J.J.1    Nguyen, B.L.2    Bridger, R.3    Medrano, E.E.4    Wells, L.5    Pan, S.6    Sifers, R.N.7
  • 42
    • 77956963665 scopus 로고    scopus 로고
    • Inhibition of O-GlcNAcase using a potent and cellpermeable inhibitor does not induce insulin resistance in 3T3-L1 adipocytes
    • Macauley, M. S., He, Y., Gloster, T. M., Stubbs, K. A., Davies, G. J., and Vocadlo, D. J. (2010) Inhibition of O-GlcNAcase using a potent and cellpermeable inhibitor does not induce insulin resistance in 3T3-L1 adipocytes. Chem. Biol. 17, 937-948
    • (2010) Chem. Biol. , vol.17 , pp. 937-948
    • Macauley, M.S.1    He, Y.2    Gloster, T.M.3    Stubbs, K.A.4    Davies, G.J.5    Vocadlo, D.J.6
  • 43
    • 0035937189 scopus 로고    scopus 로고
    • Chromosome condensation by a human condensin complex in Xenopus egg extracts
    • Kimura, K., Cuvier, O., and Hirano, T. (2001) Chromosome condensation by a human condensin complex in Xenopus egg extracts. J. Biol. Chem. 276, 5417-5420
    • (2001) J. Biol. Chem. , vol.276 , pp. 5417-5420
    • Kimura, K.1    Cuvier, O.2    Hirano, T.3
  • 44
    • 84872184195 scopus 로고    scopus 로고
    • Phosphorylation network dynamics in the control of cell cycle transitions
    • Fisher, D., Krasinska, L., Coudreuse, D., and Novák, B. (2012) Phosphorylation network dynamics in the control of cell cycle transitions. J. Cell Sci. 125, 4703-4711
    • (2012) J. Cell Sci. , vol.125 , pp. 4703-4711
    • Fisher, D.1    Krasinska, L.2    Coudreuse, D.3    Novák, B.4
  • 45
    • 0027538301 scopus 로고
    • Dephosphorylation of cdc25-C by a type-2A protein phosphatase: Specific regulation during the cell cycle in Xenopus egg extracts
    • Clarke, P. R., Hoffmann, I., Draetta, G., and Karsenti, E. (1993) Dephosphorylation of cdc25-C by a type-2A protein phosphatase: specific regulation during the cell cycle in Xenopus egg extracts. Mol. Biol. Cell 4, 397-411
    • (1993) Mol. Biol. Cell , vol.4 , pp. 397-411
    • Clarke, P.R.1    Hoffmann, I.2    Draetta, G.3    Karsenti, E.4
  • 46
    • 0028998865 scopus 로고
    • Cell cycle regulation of a Xenopus Wee1-like kinase
    • Mueller, P. R., Coleman, T. R., and Dunphy, W. G. (1995) Cell cycle regulation of a Xenopus Wee1-like kinase. Mol. Biol. Cell 6, 119-134
    • (1995) Mol. Biol. Cell , vol.6 , pp. 119-134
    • Mueller, P.R.1    Coleman, T.R.2    Dunphy, W.G.3
  • 48
    • 69249155637 scopus 로고    scopus 로고
    • Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification
    • Dias, W. B., Cheung, W. D., Wang, Z., and Hart, G. W. (2009) Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification. J. Biol. Chem. 284, 21327-21337
    • (2009) J. Biol. Chem. , vol.284 , pp. 21327-21337
    • Dias, W.B.1    Cheung, W.D.2    Wang, Z.3    Hart, G.W.4
  • 50
    • 58049197848 scopus 로고    scopus 로고
    • Elevation of global O-GlcNAc levels in 3T3-L1 adipocytes by selective inhibition of O-GlcNAcase does not induce insulin resistance
    • Macauley, M. S., Bubb, A. K., Martinez-Fleites, C., Davies, G. J., and Vocadlo, D. J. (2008) Elevation of global O-GlcNAc levels in 3T3-L1 adipocytes by selective inhibition of O-GlcNAcase does not induce insulin resistance. J. Biol. Chem. 283, 34687-34695
    • (2008) J. Biol. Chem. , vol.283 , pp. 34687-34695
    • Macauley, M.S.1    Bubb, A.K.2    Martinez-Fleites, C.3    Davies, G.J.4    Vocadlo, D.J.5
  • 51
    • 57749088688 scopus 로고    scopus 로고
    • O-linked α-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins
    • Cheung, W. D., Sakabe, K., Housley, M. P., Dias, W. B., and Hart, G. W. (2008) O-linked α-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins. J. Biol. Chem. 283, 33935-33941
    • (2008) J. Biol. Chem. , vol.283 , pp. 33935-33941
    • Cheung, W.D.1    Sakabe, K.2    Housley, M.P.3    Dias, W.B.4    Hart, G.W.5


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