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Volumn 2, Issue 4, 2011, Pages 283-288

Coordinating postmitotic nuclear pore complex assembly with abscission timing

Author keywords

Abscission; Aurora B; Cytokinesis; Nuclear basket; Nuclear pore assembly; Nuclear pore complex; Nup153; Nup50; Tpr

Indexed keywords

AURORA B KINASE; CELL PROTEIN; NUP153 PROTEIN; UNCLASSIFIED DRUG;

EID: 83455200038     PISSN: 19491034     EISSN: 19491042     Source Type: Journal    
DOI: 10.4161/nucl.2.4.16189     Document Type: Article
Times cited : (17)

References (64)
  • 1
    • 75149140916 scopus 로고    scopus 로고
    • Mitotic chromosomal instability and cancer: Mouse modelling of the human disease
    • Schvartzman JM, Sotillo R, Benezra R. Mitotic chromosomal instability and cancer: mouse modelling of the human disease. Nat Rev Cancer 2010; 10:102-15.
    • (2010) Nat Rev Cancer , vol.10 , pp. 102-115
    • Schvartzman, J.M.1    Sotillo, R.2    Benezra, R.3
  • 2
    • 34247333444 scopus 로고    scopus 로고
    • The spindle-assembly checkpoint in space and time
    • Musacchio A, Salmon ED. The spindle-assembly checkpoint in space and time. Nat Rev Mol Cell Biol 2007; 8:379-93.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 379-393
    • Musacchio, A.1    Salmon, E.D.2
  • 3
    • 73549109858 scopus 로고    scopus 로고
    • Safeguarding entry into mitosis: The antephase checkpoint
    • Chin CF, Yeong FM. Safeguarding entry into mitosis: the antephase checkpoint. Mol Cell Biol 2010; 30:22-32.
    • (2010) Mol Cell Biol , vol.30 , pp. 22-32
    • Chin, C.F.1    Yeong, F.M.2
  • 4
    • 59049094551 scopus 로고    scopus 로고
    • A last-minute rescue of trapped chromatin
    • Chen CT, Doxsey S. A last-minute rescue of trapped chromatin. Cell 2009; 136:397-9.
    • (2009) Cell , vol.136 , pp. 397-399
    • Chen, C.T.1    Doxsey, S.2
  • 5
    • 67649348147 scopus 로고    scopus 로고
    • An evolutionary conserved checkpoint controls abscission timing
    • Steigemann P, Gerlich DW. An evolutionary conserved checkpoint controls abscission timing. Cell Cycle 2009; 8:1814-5.
    • (2009) Cell Cycle , vol.8 , pp. 1814-1815
    • Steigemann, P.1    Gerlich, D.W.2
  • 6
    • 59049101302 scopus 로고    scopus 로고
    • Aurora B-mediated abscission checkpoint protects against tetraploidiza-tion
    • Steigemann P, Wurzenberger C, Schmitz MH, Held M, Guizetti J, Maar S, et al. Aurora B-mediated abscission checkpoint protects against tetraploidiza-tion. Cell 2009; 136:473-84.
    • (2009) Cell , vol.136 , pp. 473-484
    • Steigemann, P.1    Wurzenberger, C.2    Schmitz, M.H.3    Held, M.4    Guizetti, J.5    Maar, S.6
  • 7
    • 36249024229 scopus 로고    scopus 로고
    • Cytokinesis: Placing and making the final cut
    • Barr FA, Gruneberg U. Cytokinesis: placing and making the final cut. Cell 2007; 131:847-60.
    • (2007) Cell , vol.131 , pp. 847-860
    • Barr, F.A.1    Gruneberg, U.2
  • 8
    • 58049204447 scopus 로고    scopus 로고
    • The 3Ms of central spindle assembly: Microtubules, motors and MAPs
    • Glotzer M. The 3Ms of central spindle assembly: microtubules, motors and MAPs. Nat Rev Mol Cell Biol 2009; 10:9-20.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 9-20
    • Glotzer, M.1
  • 9
    • 78449270024 scopus 로고    scopus 로고
    • Cytokinetic abscission in animal cells
    • Guizetti J, Gerlich DW. Cytokinetic abscission in animal cells. Semin Cell Dev Biol 2010; 21:909-16.
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 909-916
    • Guizetti, J.1    Gerlich, D.W.2
  • 10
    • 70350343134 scopus 로고    scopus 로고
    • Cytokinetic abscission: Cellular dynamics at the midbody
    • Steigemann P, Gerlich DW. Cytokinetic abscission: cellular dynamics at the midbody. Trends Cell Biol 2009; 19:606-16.
    • (2009) Trends Cell Biol , vol.19 , pp. 606-616
    • Steigemann, P.1    Gerlich, D.W.2
  • 11
    • 33645968660 scopus 로고    scopus 로고
    • The NoCut pathway links completion of cytokinesis to spindle midzone function to prevent chromosome breakage
    • Norden C, Mendoza M, Dobbelaere J, Kotwaliwale CV, Biggins S, Barral Y. The NoCut pathway links completion of cytokinesis to spindle midzone function to prevent chromosome breakage. Cell 2006; 125:85-98.
    • (2006) Cell , vol.125 , pp. 85-98
    • Norden, C.1    Mendoza, M.2    Dobbelaere, J.3    Kotwaliwale, C.V.4    Biggins, S.5    Barral, Y.6
  • 12
    • 62149111407 scopus 로고    scopus 로고
    • Sensing chromosome bi-orientation by spatial separation of aurora B kinase from kinetochore substrates
    • Liu D, Vader G, Vromans MJ, Lampson MA, Lens SM. Sensing chromosome bi-orientation by spatial separation of aurora B kinase from kinetochore substrates. Science 2009; 323:1350-3.
    • (2009) Science , vol.323 , pp. 1350-1353
    • Liu, D.1    Vader, G.2    Vromans, M.J.3    Lampson, M.A.4    Lens, S.M.5
  • 13
    • 79954999102 scopus 로고    scopus 로고
    • Evidence that Aurora B is implicated in spindle checkpoint signalling independently of error correction
    • Santaguida S, Vernieri C, Villa F, Ciliberto A, Musacchio A. Evidence that Aurora B is implicated in spindle checkpoint signalling independently of error correction. EMBO J 2011; 30:1508-19.
    • (2011) EMBO J , vol.30 , pp. 1508-1519
    • Santaguida, S.1    Vernieri, C.2    Villa, F.3    Ciliberto, A.4    Musacchio, A.5
  • 15
    • 78649685697 scopus 로고    scopus 로고
    • Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint
    • Mackay DR, Makise M, Ullman KS. Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint. J Cell Biol 2010; 191:923-31.
    • (2010) J Cell Biol , vol.191 , pp. 923-931
    • Mackay, D.R.1    Makise, M.2    Ullman, K.S.3
  • 17
    • 65249089181 scopus 로고    scopus 로고
    • The nucleopo-rin Nup153 has separable roles in both early mitotic progression and the resolution of mitosis
    • Mackay DR, Elgort SW, Ullman KS. The nucleopo-rin Nup153 has separable roles in both early mitotic progression and the resolution of mitosis. Mol Biol Cell 2009; 20:1652-60.
    • (2009) Mol Biol Cell , vol.20 , pp. 1652-1660
    • Mackay, D.R.1    Elgort, S.W.2    Ullman, K.S.3
  • 20
    • 52949107958 scopus 로고    scopus 로고
    • Structure, dynamics and function of nuclear pore complexes
    • D'Angelo MA, Hetzer MW. Structure, dynamics and function of nuclear pore complexes. Trends Cell Biol 2008; 18:456-66.
    • (2008) Trends Cell Biol , vol.18 , pp. 456-466
    • D'angelo, M.A.1    Hetzer, M.W.2
  • 21
    • 41149157334 scopus 로고    scopus 로고
    • Sumoylating and desumoylat-ing enzymes at nuclear pores: Underpinning their unexpected duties?
    • Palancade B, Doye V. Sumoylating and desumoylat-ing enzymes at nuclear pores: underpinning their unexpected duties? Trends Cell Biol 2008; 18:174-83.
    • (2008) Trends Cell Biol , vol.18 , pp. 174-183
    • Palancade, B.1    Doye, V.2
  • 22
    • 0035887310 scopus 로고    scopus 로고
    • The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins
    • Walther TC, Fornerod M, Pickersgill H, Goldberg M, Allen TD, Mattaj IW. The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins. EMBO J 2001; 20:5703-14.
    • (2001) EMBO J , vol.20 , pp. 5703-5714
    • Walther, T.C.1    Fornerod, M.2    Pickersgill, H.3    Goldberg, M.4    Allen, T.D.5    Mattaj, I.W.6
  • 23
    • 77953893804 scopus 로고    scopus 로고
    • The nuclear pore complex: Bridging nuclear transport and gene regulation
    • Strambio-De-Castillia C, Niepel M, Rout MP. The nuclear pore complex: bridging nuclear transport and gene regulation. Nat Rev Mol Cell Biol 2010; 11:490-501.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 490-501
    • Strambio-De-Castillia, C.1    Niepel, M.2    Rout, M.P.3
  • 25
    • 0035063690 scopus 로고    scopus 로고
    • Mitotic checkpoint proteins HsMAD1 and HsMAD2 are associated with nuclear pore complexes in interphase
    • Campbell MS, Chan GK, Yen TJ. Mitotic checkpoint proteins HsMAD1 and HsMAD2 are associated with nuclear pore complexes in interphase. J Cell Sci 2001; 114:953-63.
    • (2001) J Cell Sci , vol.114 , pp. 953-963
    • Campbell, M.S.1    Chan, G.K.2    Yen, T.J.3
  • 26
    • 56949083763 scopus 로고    scopus 로고
    • Reorganization of the nuclear envelope during open mitosis
    • Kutay U, Hetzer M W. Reorganization of the nuclear envelope during open mitosis. Curr Opin Cell Biol 2008; 20:669-77.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 669-677
    • Kutay, U.1    Hetzer, M.W.2
  • 27
    • 30844455364 scopus 로고    scopus 로고
    • The nuclear envelope: Form and reformation
    • Prunuske AJ, Ullman KS. The nuclear envelope: form and reformation. Curr Opin Cell Biol 2006; 18:108-116.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 108-116
    • Prunuske, A.J.1    Ullman, K.S.2
  • 28
    • 79952333966 scopus 로고    scopus 로고
    • Nup98 regulates bipolar spindle assembly through association with microtu-bules and opposition of MCAK
    • Cross MK, Powers MA. Nup98 regulates bipolar spindle assembly through association with microtu-bules and opposition of MCAK. Mol Biol Cell 2011; 22: 661-72.
    • (2011) Mol Biol Cell , vol.22 , pp. 661-672
    • Cross, M.K.1    Powers, M.A.2
  • 30
    • 0141545024 scopus 로고    scopus 로고
    • Nup358 integrates nuclear envelope breakdown with kineto-chore assembly
    • Salina D, Enarson P, Rattner JB, Burke B. Nup358 integrates nuclear envelope breakdown with kineto-chore assembly. J Cell Biol 2003; 162:991-1001.
    • (2003) J Cell Biol , vol.162 , pp. 991-1001
    • Salina, D.1    Enarson, P.2    Rattner, J.B.3    Burke, B.4
  • 31
    • 34247272580 scopus 로고    scopus 로고
    • The human Nup107-160 nuclear pore subcomplex contributes to proper kinetochore functions
    • Zuccolo M, Alves A, Galy V, Bolhy S, Formstecher E, Racine V, et al. The human Nup107-160 nuclear pore subcomplex contributes to proper kinetochore functions. EMBO J 2007; 26:1853-64.
    • (2007) EMBO J , vol.26 , pp. 1853-1864
    • Zuccolo, M.1    Alves, A.2    Galy, V.3    Bolhy, S.4    Formstecher, E.5    Racine, V.6
  • 32
    • 41149146735 scopus 로고    scopus 로고
    • Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha
    • Dawlaty MM, Malureanu L, Jeganathan KB, Kao E, Sustmann C, Tahk S, et al. Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha. Cell 2008; 133:103-15.
    • (2008) Cell , vol.133 , pp. 103-115
    • Dawlaty, M.M.1    Malureanu, L.2    Jeganathan, K.B.3    Kao, E.4    Sustmann, C.5    Tahk, S.6
  • 33
    • 1842715846 scopus 로고    scopus 로고
    • The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo
    • Joseph J, Liu ST, Jablonski SA, Yen TJ, Dasso M. The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo. Curr Biol 2004; 14:611-7.
    • (2004) Curr Biol , vol.14 , pp. 611-617
    • Joseph, J.1    Liu, S.T.2    Jablonski, S.A.3    Yen, T.J.4    Dasso, M.5
  • 34
    • 77951209602 scopus 로고    scopus 로고
    • Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis
    • Nakano H, Funasaka T, Hashizume C, Wong RW. Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis. J Biol Chem 2010; 285:10841-9.
    • (2010) J Biol Chem , vol.285 , pp. 10841-10849
    • Nakano, H.1    Funasaka, T.2    Hashizume, C.3    Wong, R.W.4
  • 35
    • 30744477013 scopus 로고    scopus 로고
    • The Rae1-Nup98 complex prevents aneuploidy by inhibiting securin degradation
    • Jeganathan KB, Malureanu L, van Deursen JM. The Rae1-Nup98 complex prevents aneuploidy by inhibiting securin degradation. Nature 2005; 438:1036-9.
    • (2005) Nature , vol.438 , pp. 1036-1039
    • Jeganathan, K.B.1    Malureanu, L.2    van Deursen, J.M.3
  • 36
    • 40849097593 scopus 로고    scopus 로고
    • Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cells
    • Dultz E, Zanin E, Wurzenberger C, Braun M, Rabut G, Sironi L, et al. Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cells. J Cell Biol 2008; 180:857-65.
    • (2008) J Cell Biol , vol.180 , pp. 857-865
    • Dultz, E.1    Zanin, E.2    Wurzenberger, C.3    Braun, M.4    Rabut, G.5    Sironi, L.6
  • 37
    • 33947270331 scopus 로고    scopus 로고
    • MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly
    • Franz C, Walczak R, Yavuz S, Santarella R, Gentzel M, Askjaer P, et al. MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO Rep 2007; 8:165-72.
    • (2007) EMBO Rep , vol.8 , pp. 165-172
    • Franz, C.1    Walczak, R.2    Yavuz, S.3    Santarella, R.4    Gentzel, M.5    Askjaer, P.6
  • 38
    • 55549131172 scopus 로고    scopus 로고
    • Capture of AT-rich chromatin by ELYS recruits POM121 and NDC1 to initiate nuclear pore assembly
    • Rasala BA, Ramos C, Harel A, Forbes DJ. Capture of AT-rich chromatin by ELYS recruits POM121 and NDC1 to initiate nuclear pore assembly. Mol Biol Cell 2008; 19:3982-96.
    • (2008) Mol Biol Cell , vol.19 , pp. 3982-3996
    • Rasala, B.A.1    Ramos, C.2    Harel, A.3    Forbes, D.J.4
  • 39
    • 77953724768 scopus 로고    scopus 로고
    • Cell cycle-dependent differences in nuclear pore complex assembly in metazoa
    • Doucet CM, Talamas JA, Hetzer M W. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell 2010; 141:1030-41.
    • (2010) Cell , vol.141 , pp. 1030-1041
    • Doucet, C.M.1    Talamas, J.A.2    Hetzer, M.W.3
  • 40
    • 77957743829 scopus 로고    scopus 로고
    • Live imaging of single nuclear pores reveals unique assembly kinetics and mechanism in interphase
    • Dultz E, Ellenberg J. Live imaging of single nuclear pores reveals unique assembly kinetics and mechanism in interphase. J Cell Biol 2010; 191:15-22.
    • (2010) J Cell Biol , vol.191 , pp. 15-22
    • Dultz, E.1    Ellenberg, J.2
  • 41
    • 79953296849 scopus 로고    scopus 로고
    • Localization of Pom121 to the inner nuclear membrane is required for an early step of interphase nuclear pore complex assembly
    • Funakoshi T, Clever M, Watanabe A, Imamoto N. Localization of Pom121 to the inner nuclear membrane is required for an early step of interphase nuclear pore complex assembly. Mol Biol Cell 2011; 22:1058-69.
    • (2011) Mol Biol Cell , vol.22 , pp. 1058-1069
    • Funakoshi, T.1    Clever, M.2    Watanabe, A.3    Imamoto, N.4
  • 42
    • 77956338708 scopus 로고    scopus 로고
    • Nuclear pore formation but not nuclear growth is governed by cyclin-dependent kinases (Cdks) during interphase
    • Maeshima K, Iino H, Hihara S, Funakoshi T, Watanabe A, Nishimura M, et al. Nuclear pore formation but not nuclear growth is governed by cyclin-dependent kinases (Cdks) during interphase. Nat Struct Mol Biol 2010; 17:1065-71.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1065-1071
    • Maeshima, K.1    Iino, H.2    Hihara, S.3    Funakoshi, T.4    Watanabe, A.5    Nishimura, M.6
  • 43
    • 0038586471 scopus 로고    scopus 로고
    • Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex
    • Hase ME, Cordes VC. Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex. Mol Biol Cell 2003; 14:1923-1940.
    • (2003) Mol Biol Cell , vol.14 , pp. 1923-1940
    • Hase, M.E.1    Cordes, V.C.2
  • 44
    • 70349795274 scopus 로고    scopus 로고
    • Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport
    • Kosako H, Yamaguchi N, Aranami C, Ushiyama M, Kose S, Imamoto N, et al. Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport. Nat Struct Mol Biol 2009; 16:1026-35.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1026-1035
    • Kosako, H.1    Yamaguchi, N.2    Aranami, C.3    Ushiyama, M.4    Kose, S.5    Imamoto, N.6
  • 45
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import
    • Ben-Efraim I, Gerace L. Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import. J Cell Biol 2001; 152:411-7.
    • (2001) J Cell Biol , vol.152 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 46
    • 0032489840 scopus 로고    scopus 로고
    • Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr
    • Shah S, Tugendreich S, Forbes D. Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr. J Cell Biol 1998; 141:31-49.
    • (1998) J Cell Biol , vol.141 , pp. 31-49
    • Shah, S.1    Tugendreich, S.2    Forbes, D.3
  • 47
    • 0030930859 scopus 로고    scopus 로고
    • RanGTP-mediated nuclear export of karyopherin alpha involves its interaction with the nucleoporin Nup153
    • Moroianu J, Blobel G, Radu A. RanGTP-mediated nuclear export of karyopherin alpha involves its interaction with the nucleoporin Nup153. Proc Natl Acad Sci USA 1997; 94:9699-704.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9699-9704
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 48
    • 0034254413 scopus 로고    scopus 로고
    • Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: Evidence from cell-free extracts of Xenopus eggs
    • Smythe C, Jenkins HE, Hutchison CJ. Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: evidence from cell-free extracts of Xenopus eggs. EMBO J 2000; 19:3918-31.
    • (2000) EMBO J , vol.19 , pp. 3918-3931
    • Smythe, C.1    Jenkins, H.E.2    Hutchison, C.J.3
  • 49
    • 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; 279:692-703.
    • (2004) J Biol Chem , vol.279 , pp. 692-703
    • Bailey, D.1    O'Hare, P.2
  • 50
    • 0036724599 scopus 로고    scopus 로고
    • Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex
    • Zhang H, Saitoh H, Matunis MJ. Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. Mol Cell Biol 2002; 22:6498-508.
    • (2002) Mol Cell Biol , vol.22 , pp. 6498-6508
    • Zhang, H.1    Saitoh, H.2    Matunis, M.J.3
  • 51
    • 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; 277:19961-6.
    • (2002) J Biol Chem , vol.277 , pp. 19961-19966
    • Hang, J.1    Dasso, M.2
  • 52
    • 55749104738 scopus 로고    scopus 로고
    • Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint
    • Lee SH, Sterling H, Burlingame A, McCormick F. Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint. Genes Dev 2008; 22:2926-31.
    • (2008) Genes Dev , vol.22 , pp. 2926-2931
    • Lee, S.H.1    Sterling, H.2    Burlingame, A.3    McCormick, F.4
  • 53
    • 77954177001 scopus 로고    scopus 로고
    • The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1
    • Lussi YC, Shumaker DK, Shimi T, Fahrenkrog B. The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1. Nucleus 2010; 1:71-84.
    • (2010) Nucleus , vol.1 , pp. 71-84
    • Lussi, Y.C.1    Shumaker, D.K.2    Shimi, T.3    Fahrenkrog, B.4
  • 55
    • 40849115019 scopus 로고    scopus 로고
    • SUMO-2/3 modification and binding regulate the association of CENP-E with kineto-chores and progression through mitosis
    • Zhang XD, Goeres J, Zhang H, Yen TJ, Porter AC, Matunis MJ. SUMO-2/3 modification and binding regulate the association of CENP-E with kineto-chores and progression through mitosis. Mol Cell 2008; 29:729-41.
    • (2008) Mol Cell , vol.29 , 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
  • 56
    • 77949762923 scopus 로고    scopus 로고
    • Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase
    • Liu D, Vleugel M, Backer CB, Hori T, Fukagawa T, Cheeseman IM, et al. Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase. J Cell Biol 2010; 188:809-20.
    • (2010) J Cell Biol , vol.188 , pp. 809-820
    • Liu, D.1    Vleugel, M.2    Backer, C.B.3    Hori, T.4    Fukagawa, T.5    Cheeseman, I.M.6
  • 57
    • 85047696924 scopus 로고    scopus 로고
    • Aurora-B associated protein phosphatases as negative regulators of kinase activation
    • Sugiyama K, Sugiura K, Hara T, Sugimoto K, Shima H, Honda K, et al. Aurora-B associated protein phosphatases as negative regulators of kinase activation. Oncogene 2002; 21:3103-11.
    • (2002) Oncogene , vol.21 , pp. 3103-3111
    • Sugiyama, K.1    Sugiura, K.2    Hara, T.3    Sugimoto, K.4    Shima, H.5    Honda, K.6
  • 59
    • 75749117571 scopus 로고    scopus 로고
    • Nucleoporins directly stimulate expression of developmental and cell cycle genes inside the nucleoplasm
    • Kalverda B, Pickersgill H, Shloma V V, Fornerod M. Nucleoporins directly stimulate expression of developmental and cell cycle genes inside the nucleoplasm. Cell 2010; 140:360-71.
    • (2010) Cell , vol.140 , pp. 360-371
    • Kalverda, B.1    Pickersgill, H.2    Shloma, V.V.3    Fornerod, M.4
  • 60
    • 77954818442 scopus 로고    scopus 로고
    • Genome-nuclear lamina interactions and gene regulation
    • Kind J, van Steensel B. Genome-nuclear lamina interactions and gene regulation. Curr Opin Cell Biol 2010; 22:320-5.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 320-325
    • Kind, J.1    van Steensel, B.2
  • 61
    • 73849084214 scopus 로고    scopus 로고
    • The Nup107-160 nucleo-porin complex promotes mitotic events via control of the localization state of the chromosome passenger complex
    • Platani M, Santarella-Mellwig R, Posch M, Walczak R, Swedlow JR, Mattaj IW. The Nup107-160 nucleo-porin complex promotes mitotic events via control of the localization state of the chromosome passenger complex. Mol Biol Cell 2009; 20:5260-75.
    • (2009) Mol Biol Cell , vol.20 , pp. 5260-5275
    • Platani, M.1    Santarella-Mellwig, R.2    Posch, M.3    Walczak, R.4    Swedlow, J.R.5    Mattaj, I.W.6
  • 62
    • 33845227470 scopus 로고    scopus 로고
    • ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division
    • Rasala BA, Orjalo AV, Shen Z, Briggs S, Forbes DJ. ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division. Proc Natl Acad Sci USA 2006; 103:17801-6.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17801-17806
    • Rasala, B.A.1    Orjalo, A.V.2    Shen, Z.3    Briggs, S.4    Forbes, D.J.5
  • 63
    • 18244401885 scopus 로고    scopus 로고
    • Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex
    • Hawryluk-Gara LA, Shibuya EK, Wozniak RW. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Mol Biol Cell 2005; 16:2382-94.
    • (2005) Mol Biol Cell , vol.16 , pp. 2382-2394
    • Hawryluk-Gara, L.A.1    Shibuya, E.K.2    Wozniak, R.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.