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Volumn 203, Issue 6, 2013, Pages 957-969

KNL1 facilitates phosphorylation of outer kinetochore proteins by promoting Aurora B kinase activity

Author keywords

[No Author keywords available]

Indexed keywords

AURKB PROTEIN, HUMAN; AURORA B KINASE; BUB1 PROTEIN, HUMAN; CASC5 PROTEIN, HUMAN; MICROTUBULE ASSOCIATED PROTEIN; NDC80 PROTEIN, HUMAN; NUCLEAR PROTEIN; PROTEIN SERINE THREONINE KINASE;

EID: 84897943762     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201306054     Document Type: Article
Times cited : (58)

References (46)
  • 1
    • 0033106222 scopus 로고    scopus 로고
    • The conserved protein kinase Ip11 regulates microtubule binding to kinetochores in budding yeast
    • Biggins, S., F.F. Severin, N. Bhalla, I. Sassoon, A.A. Hyman, and A.W. Murray. 1999. The conserved protein kinase Ip11 regulates microtubule binding to kinetochores in budding yeast. Genes Dev. 13:532-544. http://dx.doi.org/10.1101/gad.13.5.532
    • (1999) Genes Dev , vol.13 , pp. 532-544
    • Biggins, S.1    Severin, F.F.2    Bhalla, N.3    Sassoon, I.4    Hyman, A.A.5    Murray, A.W.6
  • 3
    • 84877575218 scopus 로고    scopus 로고
    • Tension sensing by Aurora B kinase is independent of survivin-based centromere localization
    • Campbell, C.S., and A. Desai. 2013. Tension sensing by Aurora B kinase is independent of survivin-based centromere localization. Nature. 497:118-121. http://dx.doi.org/10.1038/nature12057
    • (2013) Nature , vol.497 , pp. 118-121
    • Campbell, C.S.1    Desai, A.2
  • 4
    • 33751232957 scopus 로고    scopus 로고
    • The conserved KMN network constitutes the core microtubule-binding site of the kinetochore
    • Cheeseman, I.M., J.S. Chappie, E.M. Wilson-Kubalek, and A. Desai. 2006. The conserved KMN network constitutes the core microtubule-binding site of the kinetochore. Cell. 127:983-997. http://dx.doi.org/10.1016/j.cell.2006.09.039
    • (2006) Cell , vol.127 , pp. 983-997
    • Cheeseman, I.M.1    Chappie, J.S.2    Wilson-Kubalek, E.M.3    Desai, A.4
  • 5
    • 39449096363 scopus 로고    scopus 로고
    • KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly in vertebrates
    • Cheeseman, I.M., T. Hori, T. Fukagawa, and A. Desai. 2008. KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly in vertebrates. Mol. Biol. Cell. 19:587-594. http://dx.doi.org/10.1091/mbc.E07-10-1051
    • (2008) Mol. Biol. Cell , vol.19 , pp. 587-594
    • Cheeseman, I.M.1    Hori, T.2    Fukagawa, T.3    Desai, A.4
  • 6
    • 33750612373 scopus 로고    scopus 로고
    • Aurora kinase promotes turnover of kinetochore microtubules to reduce chromosome segregation errors
    • Cimini, D., X. Wan, C.B. Hirel, and E.D. Salmon. 2006. Aurora kinase promotes turnover of kinetochore microtubules to reduce chromosome segregation errors. Curr. Biol. 16:1711-1718. http://dx.doi.org/10.1016/j.cub.2006.07.022
    • (2006) Curr. Biol , vol.16 , pp. 1711-1718
    • Cimini, D.1    Wan, X.2    Hirel, C.B.3    Salmon, E.D.4
  • 7
  • 8
    • 33751227843 scopus 로고    scopus 로고
    • Kinetochore microtubule dynamics and attachment stability are regulated by Hec1
    • DeLuca, J.G., W.E. Gall, C. Ciferri, D. Cimini, A. Musacchio, and E.D. Salmon. 2006. Kinetochore microtubule dynamics and attachment stability are regulated by Hec1. Cell. 127:969-982. http://dx.doi.org/10.1016/j.cell.2006.09.047
    • (2006) Cell , vol.127 , pp. 969-982
    • DeLuca, J.G.1    Gall, W.E.2    Ciferri, C.3    Cimini, D.4    Musacchio, A.5    Salmon, E.D.6
  • 9
    • 79951833036 scopus 로고    scopus 로고
    • Temporal changes in Hec1 phosphorylation control kinetochore-microtubule attachment stability during mitosis
    • DeLuca, K.F., S.M. Lens, and J.G. DeLuca. 2011. Temporal changes in Hec1 phosphorylation control kinetochore-microtubule attachment stability during mitosis. J. Cell Sci. 124:622-634. http://dx.doi.org/10.1242/jcs.072629
    • (2011) J. Cell Sci , vol.124 , pp. 622-634
    • DeLuca, K.F.1    Lens, S.M.2    DeLuca, J.G.3
  • 10
    • 0141818005 scopus 로고    scopus 로고
    • KNL-1 directs assembly of the microtubule-binding interface of the kinetochore in C. elegans
    • Desai, A., S. Rybina, T. Müller-Reichert, A. Shevchenko, A. Shevchenko, A. Hyman, and K. Oegema. 2003. KNL-1 directs assembly of the microtubule-binding interface of the kinetochore in C. elegans. Genes Dev. 17:2421-2435. http://dx.doi.org/10.1101/gad.1126303
    • (2003) Genes Dev. , vol.17 , pp. 2421-2435
    • Desai, A.1    Rybina, S.2    Müller-Reichert, T.3    Shevchenko, A.4    Shevchenko, A.5    Hyman, A.6    Oegema, K.7
  • 11
    • 84859941751 scopus 로고    scopus 로고
    • Microtubule binding by KNL-1 contributes to spindle checkpoint silencing at the kinetochore
    • Espeut, J., D.K. Cheerambathur, L. Krenning, K. Oegema, and A. Desai. 2012. Microtubule binding by KNL-1 contributes to spindle checkpoint silencing at the kinetochore. J. Cell Biol. 196:469-482. http://dx.doi.org/10.1083/jcb.201111107
    • (2012) J. Cell Biol , vol.196 , pp. 469-482
    • Espeut, J.1    Cheerambathur, D.K.2    Krenning, L.3    Oegema, K.4    Desai, A.5
  • 12
    • 80053573427 scopus 로고    scopus 로고
    • Formation of stable attachments between kinetochores and microtubules depends on the B56-PP2A phosphatase
    • Foley, E.A., M. Maldonado, and T.M. Kapoor. 2011. Formation of stable attachments between kinetochores and microtubules depends on the B56-PP2A phosphatase. Nat. Cell Biol. 13:1265-1271. http://dx.doi.org/10.1038/ncb2327
    • (2011) Nat. Cell Biol , vol.13 , pp. 1265-1271
    • Foley, E.A.1    Maldonado, M.2    Kapoor, T.M.3
  • 13
    • 0035153295 scopus 로고    scopus 로고
    • Microtubule-dependent changes in assembly of microtubule motor proteins and mitotic spindle checkpoint proteins at PtK1 kinetochores
    • Hoffman, D.B., C.G. Pearson, T.J. Yen, B.J. Howell, and E.D. Salmon. 2001. Microtubule-dependent changes in assembly of microtubule motor proteins and mitotic spindle checkpoint proteins at PtK1 kinetochores. Mol. Biol. Cell. 12:1995-2009. http://dx.doi.org/10.1091/mbc.12.7.1995
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1995-2009
    • Hoffman, D.B.1    Pearson, C.G.2    Yen, T.J.3    Howell, B.J.4    Salmon, E.D.5
  • 14
    • 0041968963 scopus 로고    scopus 로고
    • Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis
    • Honda, R.K., R. Körner, and E.A. Nigg. 2003. Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis. Mol. Biol. Cell. 14:3325-3341. http://dx.doi.org/10.1091/mbc.E02-11-0769
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3325-3341
    • Honda, R.K.1    Körner, R.2    Nigg, E.A.3
  • 15
    • 74249093169 scopus 로고    scopus 로고
    • Phosphorylation of H2A by Bub1 prevents chromosomal instability through localizing shugoshin
    • Kawashima, S.A., Y. Yamagishi, T. Honda, K. Ishiguro, and Y. Watanabe. 2010. Phosphorylation of H2A by Bub1 prevents chromosomal instability through localizing shugoshin. Science. 327:172-177. http://dx.doi.org/10.1126/science.1180189
    • (2010) Science , vol.327 , pp. 172-177
    • Kawashima, S.A.1    Yamagishi, Y.2    Honda, T.3    Ishiguro, K.4    Watanabe, Y.5
  • 16
    • 35649019314 scopus 로고    scopus 로고
    • Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic checkpoint through direct interaction with Bub1 and BubR1
    • Kiyomitsu, T., C. Obuse, and M. Yanagida. 2007. Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic checkpoint through direct interaction with Bub1 and BubR1. Dev. Cell. 13:663-676. http://dx.doi.org/10.1016/j.devcel.2007.09.005
    • (2007) Dev. Cell , vol.13 , pp. 663-676
    • Kiyomitsu, T.1    Obuse, C.2    Yanagida, M.3
  • 17
    • 79952269227 scopus 로고    scopus 로고
    • Protein interaction domain mapping of human kinetochore protein Blinkin reveals a consensus motif for binding of spindle assembly checkpoint proteins Bub1 and BubR1
    • Kiyomitsu, T., H. Murakami, and M. Yanagida. 2011. Protein interaction domain mapping of human kinetochore protein Blinkin reveals a consensus motif for binding of spindle assembly checkpoint proteins Bub1 and BubR1. Mol. Cell. Biol. 31:998-1011. http://dx.doi.org/10.1128/MCB.00815-10
    • (2011) Mol. Cell. Biol , vol.31 , pp. 998-1011
    • Kiyomitsu, T.1    Murakami, H.2    Yanagida, M.3
  • 18
    • 66349124679 scopus 로고    scopus 로고
    • Bub1 regulates chromosome segregation in a kinetochore-independent manner
    • Klebig, C., D. Korinth, and P. Meraldi. 2009. Bub1 regulates chromosome segregation in a kinetochore-independent manner. J. Cell Biol. 185:841-858. http://dx.doi.org/10.1083/jcb.200902128
    • (2009) J. Cell Biol , vol.185 , pp. 841-858
    • Klebig, C.1    Korinth, D.2    Meraldi, P.3
  • 19
    • 33645730743 scopus 로고    scopus 로고
    • The human Mis12 complex is required for kinetochore assembly and proper chromosome segregation
    • Kline, S.L., I.M. Cheeseman, T. Hori, T. Fukagawa, and A. Desai. 2006. The human Mis12 complex is required for kinetochore assembly and proper chromosome segregation. J. Cell Biol. 173:9-17. http://dx.doi.org/10.1083/jcb.200509158
    • (2006) J. Cell Biol , vol.173 , pp. 9-17
    • Kline, S.L.1    Cheeseman, I.M.2    Hori, T.3    Fukagawa, T.4    Desai, A.5
  • 20
    • 84859983402 scopus 로고    scopus 로고
    • Structural analysis reveals features of the spindle checkpoint kinase Bub1-kinetochore subunit Kn11 interaction
    • Krenn, V., A. Wehenkel, X. Li, S. Santaguida, and A. Musacchio. 2012. Structural analysis reveals features of the spindle checkpoint kinase Bub1-kinetochore subunit Kn11 interaction. J. Cell Biol. 196:451-467. http://dx.doi.org/10.1083/jcb.201110013
    • (2012) J. Cell Biol , vol.196 , pp. 451-467
    • Krenn, V.1    Wehenkel, A.2    Li, X.3    Santaguida, S.4    Musacchio, A.5
  • 22
    • 12344266713 scopus 로고    scopus 로고
    • The human mitotic checkpoint protein BubR1 regulates chromosome-spindle attachments
    • Lampson, M.A., and T.M. Kapoor. 2005. The human mitotic checkpoint protein BubR1 regulates chromosome-spindle attachments. Nat. Cell Biol. 7:93-98. http://dx.doi.org/10.1038/ncb1208
    • (2005) Nat. Cell Biol. , vol.7 , pp. 93-98
    • Lampson, M.A.1    Kapoor, T.M.2
  • 23
    • 61349161193 scopus 로고    scopus 로고
    • Model for protein concentration gradients in the cytoplasm
    • Lipkow, K., and D.J. Odde. 2008. Model for protein concentration gradients in the cytoplasm. Cell Mol Bioeng. 1:84-92. http://dx.doi.org/10.1007/s12195-008-0008-8
    • (2008) Cell Mol Bioeng , vol.1 , pp. 84-92
    • Lipkow, K.1    Odde, D.J.2
  • 24
    • 62149111407 scopus 로고    scopus 로고
    • Sensing chromosome bi-orientation by spatial separation of aurora B kinase from kinetochore substrates
    • Liu, D., G. Vader, M.J. Vromans, M.A. Lampson, and S.M. Lens. 2009. Sensing chromosome bi-orientation by spatial separation of aurora B kinase from kinetochore substrates. Science. 323:1350-1353. http://dx.doi.org/10.1126/science.1167000
    • (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
  • 25
    • 77949762923 scopus 로고    scopus 로고
    • Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase
    • Liu, D., M. Vleugel, C.B. Backer, T. Hori, T. Fukagawa, I.M. Cheeseman, and M.A. Lampson. 2010. Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase. J. Cell Biol. 188:809-820. http://dx.doi.org/10.1083/jcb.201001006
    • (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    Lampson, M.A.7
  • 26
    • 84861532305 scopus 로고    scopus 로고
    • Phosphoregulation of Spc105 by Mps1 and PP1 regulates Bub1 localization to kinetochores
    • London, N., S. Ceto, J.A. Ranish, and S. Biggins. 2012. Phosphoregulation of Spc105 by Mps1 and PP1 regulates Bub1 localization to kinetochores. Curr. Biol. 22:900-906. http://dx.doi.org/10.1016/j.cub.2012.03.052
    • (2012) Curr. Biol , vol.22 , pp. 900-906
    • London, N.1    Ceto, S.2    Ranish, J.A.3    Biggins, S.4
  • 28
    • 81055155447 scopus 로고    scopus 로고
    • Spindle assembly checkpoint: The third decade
    • Musacchio, A. 2011. Spindle assembly checkpoint: the third decade. Philos. Trans. R. Soc. Lond. B Biol. Sci. 366:3595-3604. http://dx.doi.org/10.1098/rstb.2011.0072
    • (2011) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.366 , pp. 3595-3604
    • Musacchio, A.1
  • 29
    • 84855724543 scopus 로고    scopus 로고
    • Phosphorylation at serine 331 is required for Aurora B activation
    • Petsalaki, E., T. Akoumianaki, E.J. Black, D.A. Gillespie, and G. Zachos. 2011. Phosphorylation at serine 331 is required for Aurora B activation. J. Cell Biol. 195:449-466. http://dx.doi.org/10.1083/jcb.201104023
    • (2011) J. Cell Biol , vol.195 , pp. 449-466
    • Petsalaki, E.1    Akoumianaki, T.2    Black, E.J.3    Gillespie, D.A.4    Zachos, G.5
  • 30
    • 77957731871 scopus 로고    scopus 로고
    • Sds22 regulates aurora B activity and microtubulekinetochore interactions at mitosis
    • Posch, M., G.A. Khoudoli, S. Swift, E.M. King, J.G. Deluca, and J.R. Swedlow. 2010. Sds22 regulates aurora B activity and microtubulekinetochore interactions at mitosis. J. Cell Biol. 191:61-74. http://dx.doi.org/10.1083/jcb.200912046
    • (2010) J. Cell Biol , vol.191 , pp. 61-74
    • Posch, M.1    Khoudoli, G.A.2    Swift, S.3    King, E.M.4    Deluca, J.G.5    Swedlow, J.R.6
  • 31
    • 79959416796 scopus 로고    scopus 로고
    • Bub1 overexpression induces aneuploidy and tumor formation through Aurora B kinase hyperactivation
    • Ricke, R.M., K.B. Jeganathan, and J.M. van Deursen. 2011. Bub1 overexpression induces aneuploidy and tumor formation through Aurora B kinase hyperactivation. J. Cell Biol. 193:1049-1064. http://dx.doi.org/10.1083/jcb.201012035
    • (2011) J. Cell Biol , vol.193 , pp. 1049-1064
    • Ricke, R.M.1    Jeganathan, K.B.2    van Deursen, J.M.3
  • 32
    • 84872043569 scopus 로고    scopus 로고
    • Bub1 kinase activity drives error correction and mitotic checkpoint control but not tumor suppression
    • Ricke, R.M., K.B. Jeganathan, L. Malureanu, A.M. Harrison, and J.M. van Deursen. 2012. Bub1 kinase activity drives error correction and mitotic checkpoint control but not tumor suppression. J. Cell Biol. 199:931-949. http://dx.doi.org/10.1083/jcb.201205115
    • (2012) J. Cell Biol , vol.199 , pp. 931-949
    • Ricke, R.M.1    Jeganathan, K.B.2    Malureanu, L.3    Harrison, A.M.4    van Deursen, J.M.5
  • 33
    • 0019861101 scopus 로고
    • The structure of the cold-stable kinetochore fiber in metaphase PtK1 cells
    • Rieder, C.L. 1981. The structure of the cold-stable kinetochore fiber in metaphase PtK1 cells. Chromosoma. 84:145-158. http://dx.doi.org/10.1007/BF00293368
    • (1981) Chromosoma , vol.84 , pp. 145-158
    • Rieder, C.L.1
  • 34
    • 79958021557 scopus 로고    scopus 로고
    • KNL1/Spc105 recruts PP1 to silence the spindle assembly checkpoint
    • Rosenberg, J.S., F.R. Cross, and H. Funabiki. 2011. KNL1/Spc105 recruts PP1 to silence the spindle assembly checkpoint. Curr. Biol. 21:942-947. http://dx.doi.org/10.1016/j.cub.2011.04.011
    • (2011) Curr. Biol , vol.21 , pp. 942-947
    • Rosenberg, J.S.1    Cross, F.R.2    Funabiki, H.3
  • 36
    • 79960988207 scopus 로고    scopus 로고
    • Uncoordinated loss of chromatid cohesion is a common outcome of extended metaphase arrest
    • Stevens, D., R. Gassmann, K. Oegema, and A. Desai. 2011. Uncoordinated loss of chromatid cohesion is a common outcome of extended metaphase arrest. PLoS ONE. 6: e22969. http://dx.doi.org/10.1371/journal.pone.0022969
    • (2011) PLoS ONE , vol.6 , pp. e22969
    • Stevens, D.1    Gassmann, R.2    Oegema, K.3    Desai, A.4
  • 37
    • 38849201167 scopus 로고    scopus 로고
    • The kinesin-8 motor Kif18A suppresses kinetochore movements to control mitotic chromosome alignment
    • Stumpff, J., G. von Dassow, M. Wagenbach, C. Asbury, and L. Wordeman. 2008. The kinesin-8 motor Kif18A suppresses kinetochore movements to control mitotic chromosome alignment. Dev. Cell. 14:252-262. http://dx.doi.org/10.1016/j.devcel.2007.11.014
    • (2008) Dev. Cell , vol.14 , pp. 252-262
    • Stumpff, J.1    von Dassow, G.2    Wagenbach, M.3    Asbury, C.4    Wordeman, L.5
  • 38
    • 84867673051 scopus 로고    scopus 로고
    • Integration of kinase and phosphatase activities by BUBR1 ensures formation of stable kinetochore-microtubule attachments
    • Suijkerbuijk, S.J., M. Vleugel, A. Teixeira, and G.J. Kops. 2012. Integration of kinase and phosphatase activities by BUBR1 ensures formation of stable kinetochore-microtubule attachments. Dev. Cell. 23:745-755. http://dx.doi.org/10.1016/j.devcel.2012.09.005
    • (2012) Dev. Cell , vol.23 , pp. 745-755
    • Suijkerbuijk, S.J.1    Vleugel, M.2    Teixeira, A.3    Kops, G.J.4
  • 39
    • 0036178929 scopus 로고    scopus 로고
    • Evidence that the Ip11-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections
    • Tanaka, T.U., N. Rachidi, C. Janke, G. Pereira, M. Galova, E. Schiebel, M.J. Stark, and K. Nasmyth. 2002. Evidence that the Ip11-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections. Cell. 108:317-329. http://dx.doi.org/10.1016/S0092-8674(02)00633-5
    • (2002) Cell , vol.108 , pp. 317-329
    • Tanaka, T.U.1    Rachidi, N.2    Janke, C.3    Pereira, G.4    Galova, M.5    Schiebel, E.6    Stark, M.J.7    Nasmyth, K.8
  • 40
    • 77958008898 scopus 로고    scopus 로고
    • Phosphorylation of the CPC by Cdk1 promotes chromosome bi-orientation
    • Tsukahara, T., Y. Tanno, and Y. Watanabe. 2010. Phosphorylation of the CPC by Cdk1 promotes chromosome bi-orientation. Nature. 467:719-723. http://dx.doi.org/10.1038/nature09390
    • (2010) Nature , vol.467 , pp. 719-723
    • Tsukahara, T.1    Tanno, Y.2    Watanabe, Y.3
  • 41
    • 80052621348 scopus 로고    scopus 로고
    • Aurora B dynamics at centromeres create a diffusion-based phosphorylation gradient
    • Wang, E., E.R. Ballister, and M.A. Lampson. 2011. Aurora B dynamics at centromeres create a diffusion-based phosphorylation gradient. J. Cell Biol. 194:539-549. http://dx.doi.org/10.1083/jcb.201103044
    • (2011) J. Cell Biol. , vol.194 , pp. 539-549
    • Wang, E.1    Ballister, E.R.2    Lampson, M.A.3
  • 42
    • 77951952612 scopus 로고    scopus 로고
    • Aurora B phosphorylates spatially distinct targets to differentially regulate the kinetochore-microtubule interface
    • Welburn, J.P., M. Vleugel, D. Liu, J.R. Yates III, M.A. Lampson, T. Fukagawa, and I.M. Cheeseman. 2010. Aurora B phosphorylates spatially distinct targets to differentially regulate the kinetochore-microtubule interface. Mol. Cell. 38:383-392. http://dx.doi.org/10.1016/j.molcel.2010.02.034
    • (2010) Mol. Cell , vol.38 , pp. 383-392
    • Welburn, J.P.1    Vleugel, M.2    Liu, D.3    Yates, J.R.4    Lampson, M.A.5    Fukagawa, T.6    Cheeseman, I.M.7
  • 43
    • 77957731584 scopus 로고    scopus 로고
    • Two histone marks establish the inner centromere and chromosome bi-orientation
    • Yamagishi, Y., T. Honda, Y. Tanno, and Y. Watanabe. 2010. Two histone marks establish the inner centromere and chromosome bi-orientation. Science. 330:239-243. http://dx.doi.org/10.1126/science.1194498
    • (2010) Science , vol.330 , pp. 239-243
    • Yamagishi, Y.1    Honda, T.2    Tanno, Y.3    Watanabe, Y.4
  • 44
    • 84863226706 scopus 로고    scopus 로고
    • MPS1/Mph1 phosphorylates the kinetochore protein KNL1/Spc7 to recruit SAC components
    • Yamagishi, Y., C.H. Yang, Y. Tanno, and Y. Watanabe. 2012. MPS1/Mph1 phosphorylates the kinetochore protein KNL1/Spc7 to recruit SAC components. Nat. Cell Biol. 14:746-752. http://dx.doi.org/10.1038/ncb2515
    • (2012) Nat. Cell Biol , vol.14 , pp. 746-752
    • Yamagishi, Y.1    Yang, C.H.2    Tanno, Y.3    Watanabe, Y.4
  • 46
    • 55949106979 scopus 로고    scopus 로고
    • Deconstructing Survivin: Comprehensive genetic analysis of Survivin function by conditional knockout in a vertebrate cell line
    • Yue, Z., A. Carvalho, Z. Xu, X. Yuan, S. Cardinale, S. Ribeiro, F. Lai, H. Ogawa, E. Gudmundsdottir, R. Gassmann, et al. 2008. Deconstructing Survivin: comprehensive genetic analysis of Survivin function by conditional knockout in a vertebrate cell line. J. Cell Biol. 183:279-296. http://dx.doi.org/10.1083/jcb.200806118
    • (2008) J. Cell Biol , vol.183 , pp. 279-296
    • Yue, Z.1    Carvalho, A.2    Xu, Z.3    Yuan, X.4    Cardinale, S.5    Ribeiro, S.6    Lai, F.7    Ogawa, H.8    Gudmundsdottir, E.9    Gassmann, R.10


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