On the molecular mechanisms of mitotic kinase activation

Open Biology

Volumn 2, Issue NOV, 2012, Pages

  Bayliss, Richard ^a   Fry, Andrew ^a   Haq, Tamanna ^a   Yeoh, Sharon ^b  

^a Department of Biochemistry ^*  (United Kingdom)

^b UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

Mitosis; Protein kinases; Protein structures; Regulation

Indexed keywords

CELL CYCLE PROTEIN; PROTEIN KINASE;

ANIMAL; CHEMICAL STRUCTURE; ENZYME ACTIVATION; ENZYMOLOGY; FEEDBACK SYSTEM; GENE EXPRESSION REGULATION; GENETICS; HUMAN; KINETICS; METABOLISM; MITOSIS; MITOSIS SPINDLE; NEOPLASM; PHOSPHORYLATION; PROTEIN STRUCTURES; REGULATORY MECHANISM; REVIEW; XENOPUS LAEVIS; ZEBRA FISH;

MITOSIS; PROTEIN KINASES; PROTEIN STRUCTURES; REGULATION;

ANIMALS; CELL CYCLE PROTEINS; ENZYME ACTIVATION; FEEDBACK, PHYSIOLOGICAL; GENE EXPRESSION REGULATION; HUMANS; KINETICS; MITOSIS; MITOTIC SPINDLE APPARATUS; MODELS, MOLECULAR; NEOPLASMS; PHOSPHORYLATION; PROTEIN KINASES; XENOPUS LAEVIS; ZEBRAFISH;

EID: 84874306548     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.120136     Document Type: Article

References (125)

1. Musacchio A, Salmon ED. 2007 The spindle-assembly checkpoint in space and time. Nat. Rev. Mol. Cell. Biol. 8, 379-393. (doi:10.1038/nrm2163)
2. Lengauer C, Kinzler KW, Vogelstein B. 1997 Genetic instability in colorectal cancers. Nature 386, 623-627. (doi:10.1038/386623a0)
3. Nigg EA. 2002 Centrosome aberrations: cause or consequence of cancer progression? Nat. Rev. Cancer 2, 815-825. (doi:10.1038/nrc924)
4. Kops GJ, Weaver BA, Cleveland DW. 2005 On the road to cancer: aneuploidy and the mitotic checkpoint. Nat. Rev. Cancer 5, 773-785. (doi:10.1038/nrc1714)
5. Manchado E, Guillamot M, Malumbres M. 2012 Killing cells by targeting mitosis. Cell Death Differ. 19, 369-377. (doi:10.1038/cdd.2011.197)
6. Ma HT, Poon RY. 2011 How protein kinases coordinate mitosis in animal cells. Biochem. J. 435, 17-31. (doi:10.1042/BJ20100284)
7. Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S. 2002 The protein kinase complement of the human genome. Science 298, 1912-1934. (doi:10.1126/science.1075762)
8. Hunt T. 1989 Maturation promoting factor, cyclin and the control of M-phase. Curr. Opin. Cell Biol. 1, 268-274. (doi:10.1016/0955-0674(89)90099-9)
9. Morgan DO. 1995 Principles of CDK regulation. Nature 374, 131-134. (doi:10.1038/374131a0)
10. Pavletich NP. 1999 Mechanisms of cyclin-dependent kinase regulation: structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors. J. Mol. Biol. 287, 821-828. (doi:10.1006/jmbi.1999.2640)
11. Enserink JM, Kolodner RD. 2010 An overview of Cdk1-controlled targets and processes. Cell Div. 5, 11. (doi:10.1186/1747-1028-5-11)
12. Barr FA, Sillje HH, Nigg EA. 2004 Polo-like kinases and the orchestration of cell division. Nat. Rev. Mol. Cell. Biol. 5, 429-440. (doi:10.1038/nrm1401)
13. Glover DM. 2005 Polo kinase and progression through M phase in Drosophila: a perspective from the spindle poles. Oncogene 24, 230-237. (doi:10.1038/sj.onc.1208279)
14. Lowery DM, Lim D, Yaffe MB. 2005 Structure and function of Polo-like kinases. Oncogene 24, 248-259. (doi:10.1038/sj.onc.1208280)
15. Archambault V, Carmena M. 2012 Polo-like kinase-activating kinases: aurora A, Aurora B and what else? Cell Cycle. 11, 1490-1495. (doi:10.4161/cc.19724)
16. Lindon C, Pines J. 2004 Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells. J. Cell Biol. 164, 233-241. (doi:10.1083/jcb.200309035)
17. Chan CS, Botstein D. 1993 Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast. Genetics 135, 677-691.
18. Francisco L, Chan CS. 1994 Regulation of yeast chromosome segregation by Ipl1 protein kinase and type 1 protein phosphatase. Cell Mol. Biol. Res. 40, 207-213.
19. Barr AR, Gergely F. 2007 Aurora-A: the maker and breaker of spindle poles. J. Cell Sci. 120, 2987-2996. (doi:10.1242/jcs.013136)
20. Nikonova AS, Astsaturov I, Serebriiskii IG, Dunbrack Jr RL, Golemis EA. In press. Aurora A kinase (AURKA) in normal and pathological cell division. Cell Mol. Life Sci. (doi:10.1007/s00018-012-1073-7)
21. Mori D, Yamada M, Mimori-Kiyosue Y, Shirai Y, Suzuki A, Ohno S, Saya H, Wynshaw-Boris A, Hirotsune S. 2009 An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation by modulation of microtubule dynamics. Nat. Cell. Biol. 11, 1057-1068. (doi:10.1038/ncb1919)
22. Pugacheva EN, Jablonski SA, Hartman TR, Henske EP, Golemis EA. 2007 HEF1-dependent Aurora A activation induces disassembly of the primary cilium. Cell 129, 1351-1363. (doi:10.1016/j.cell.2007.04.035)
23. Goto H, Yasui Y, Nigg EA, Inagaki M. 2002 Aurora-B phosphorylates histone H3 at serine28 with regard to the mitotic chromosome condensation. Genes Cells 7, 11-17. (doi:10.1046/j.1356-9597.2001.00498.x)
24. Lampson MA, Cheeseman IM. 2011 Sensing centromere tension: aurora B and the regulation of kinetochore function. Trends Cell Biol. 21, 133-140. (doi:10.1016/j.tcb.2010.10.007)
25. Sasai K et al. 2004 Aurora-C kinase is a novel chromosomal passenger protein that can complement Aurora-B kinase function in mitotic cells. Cell Motil. Cytoskeleton 59, 249-263. (doi:10.1002/cm.20039)
26. Carmena M, Earnshaw WC. 2003 The cellular geography of aurora kinases. Nat. Rev. Mol. Cell. Biol. 4, 842-854. (doi:10.1038/nrm1245)
27. Morris NR. 1975 Mitotic mutants of Aspergillus nidulans. Genet. Res. 26, 237-254. (doi:10.1017/S0016672300016049)
28. Morris NR, Osmani SA, Engle DB, Doonan JH. 1989 The genetic analysis of mitosis in Aspergillus nidulans. Bioessays 10, 196-201. (doi:10.1002/bies. 950100605)
29. O'Regan L, Blot J, Fry AM. 2007 Mitotic regulation by NIMA-related kinases. Cell Div. 2, 25. (doi:10.1186/1747-1028-2-25)
30. Fry AM, Arnaud L, Nigg EA. 1999 Activity of the human centrosomal kinase, Nek2, depends on an unusual leucine zipper dimerization motif. J. Biol. Chem. 274, 16304-16310. (doi:10.1074/jbc.274.23.16304)
31. Roig J, Mikhailov A, Belham C, Avruch J. 2002 Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression. Genes Dev. 16, 1640-1658. (doi:10.1101/gad.972202)
32. Fry AM, Schultz SJ, Bartek J, Nigg EA. 1995 Substrate specificity and cell cycle regulation of the Nek2 protein kinase, a potential human homolog of the mitotic regulator NIMA of Aspergillus nidulans. J. Biol. Chem. 270, 12899-12905. (doi:10.1074/jbc.270.21.12899)
33. Lu KP, Osmani SA, Means AR. 1993 Properties and regulation of the cell cycle-specific NIMA protein kinase of Aspergillus nidulans. J. Biol. Chem. 268, 8769-8776.
34. Fry AM. 2002 The Nek2 protein kinase: a novel regulator of centrosome structure. Oncogene 21, 6184-6194. (doi:10.1038/sj.onc.1205711)
35. Hames RS, Wattam SL, Yamano H, Bacchieri R, Fry AM. 2001 APC/C-mediated destruction of the centrosomal kinase Nek2A occurs in early mitosis and depends upon a cyclin A-type D-box. EMBO J. 20, 7117-7127. (doi:10.1093/emboj/20.24. 7117)
36. Hayes MJ, Kimata Y, Wattam SL, Lindon C, Mao G, Yamano H, Fry AM. 2006 Early mitotic degradation of Nek2A depends on Cdc20-independent interaction with the APC/C. Nat. Cell. Biol. 8, 607-614. (doi:10.1038/ncb1410)
37. Sdelci S, Bertran MT, Roig J. 2011 Nek9, Nek6, Nek7 and the separation of centrosomes. Cell Cycle 10, 3816-3817. (doi:10.4161/cc.10.22.18226)
38. Belham C, Roig J, Caldwell JA, Aoyama Y, Kemp BE, Comb M, Avruch J. 2003 A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the Nek6 and Nek7 kinases. J. Biol. Chem. 278, 34897-34909. (doi:10.1074/jbc.M303663200)
39. Richards MW, O'Regan L, Mas-Droux C, Blot JM, Cheung J, Hoelder S, Fry AM, Bayliss R. 2009 An autoinhibitory tyrosine motif in the cell-cycle-regulated Nek7 kinase is released through binding of Nek9. Mol. Cell. 36, 560-570. (doi:10.1016/j.molcel.2009.09.038)
40. Rapley J, Nicolas M, Groen A, Regue L, Bertran MT, Caelles C, Avruch J, Roig J. 2008 The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site necessary for mitotic spindle formation. J. Cell Sci. 121, 3912-3921. (doi:10.1242/jcs.035360)
41. Sdelci S, Schutz M, Pinyol R, Bertran MT, Regue L, Caelles C, Vernos I, Roig J. 2012 Nek9 Phosphorylation of NEDD1/GCP-WD contributes to Plk1 control of gamma-tubulin recruitment to the mitotic centrosome. Curr. Biol. 22, 1516-1523. (doi:10.1016/j.cub.2012.06.027)
42. Logarinho E, Bousbaa H. 2008 Kinetochore-microtubule interactions 'in check' by Bub1, Bub3 and BubR1: the dual task of attaching and signalling. Cell Cycle 7, 1763-1768 (doi:10.4161/cc. 7.12.6180)
43. Elowe S. 2011 Bub1 and BubR1: at the interface between chromosome attachment and the spindle checkpoint. Mol. Cell. Biol. 31, 3085-3093. (doi:10.1128/mcb.05326-11)
44. Bolanos-Garcia VM, Blundell TL. 2011 BUB1 and BUBR1: multifaceted kinases of the cell cycle. Trends Biochem. Sci. 36, 141-150. (doi:10.1016/j.tibs.2010. 08.004)
45. Bolanos-Garcia VM et al. 2009 The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores. Structure 17, 105-116. (doi:10.1016/j.str.2008.10.015)
46. Bolanos-Garcia VM et al. 2011 Structure of a Blinkin-BUBR1 complex reveals an interaction crucial for kinetochore-mitotic checkpoint regulation via an unanticipated binding site. Structure 19, 1691-1700. (doi:10.1016/j.str. 2011.09.017)
47. Larsen NA, Al-Bassam J, Wei RR, Harrison SC. 2007 Structural analysis of Bub3 interactions in the mitotic spindle checkpoint. Proc. Natl Acad. Sci. USA 104, 1201-1206. (doi:10.1073/pnas.0610358104)
48. Higgins JM. 2010 Haspin: a newly discovered regulator of mitotic chromosome behavior. Chromosoma 119, 137-147. (doi:10.1007/s00412-009-0250-4)
49. Kelly AE, Ghenoiu C, Xue JZ, Zierhut C, Kimura H, Funabiki H. 2010 Survivin reads phosphorylated histone H3 threonine 3 to activate the mitotic kinase Aurora B. Science 330, 235-239. (doi:10.1126/science.1189505)
50. Wang F, Dai J, Daum JR, Niedzialkowska E, Banerjee B, Stukenberg PT, Gorbsky GJ, Higgins JM. 2010 Histone H3 Thr-3 phosphorylation by Haspin positions Aurora B at centromeres in mitosis. Science 330, 231-235. (doi:10.1126/science.1189435)
51. Wang F, Ulyanova NP, van der Waal MS, Patnaik D, Lens SM, Higgins JM. 2011 A positive feedback loop involving Haspin and Aurora B promotes CPC accumulation at centromeres in mitosis. Curr. Biol. 21, 1061-1069. (doi:10.1016/j.cub.2011.05.016)
52. Liu X, Winey M. 2012 The MPS1 family of protein kinases. Annu. Rev. Biochem. 81, 561-585. (doi:10.1146/annurev-biochem-061611-090435)
53. Lan W, Cleveland DW. 2010 A chemical tool box defines mitotic and interphase roles for Mps1 kinase. J. Cell Biol. 190, 21-24. (doi:10.1083/jcb. 201006080)
54. Lee S, Thebault P, Freschi L, Beaufils S, Blundell TL, Landry CR, Bolanos-Garcia VM, Elowe S. 2012 Characterization of spindle checkpoint kinase Mps1 reveals domain with functional and structural similarities to tetratricopeptide repeat motifs of Bub1 and BubR1 checkpoint kinases. J. Biol. Chem. 287, 5988-6001. (doi:10.1074/jbc.M111.307355)
55. Tyler RK, Chu ML, Johnson H, McKenzie EA, Gaskell SJ, Eyers PA. 2009 Phosphoregulation of human Mps1 kinase. Biochem J. 417, 173-181. (doi:10.1042/bj20081310)
56. Cui Y, Cheng X, Zhang C, Zhang Y, Li S, Wang C, Guadagno TM. 2010 Degradation of the human mitotic checkpoint kinase Mps1 is cell cycle-regulated by APC-cCdc20 and APC-cCdh1 ubiquitin ligases. J. Biol. Chem. 285, 32988-32998. (doi:10.1074/jbc.M110.140905)
57. Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, Sowadski JM. 1991 Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414. (doi:10.1126/science.1862342)
58. Huse M, Kuriyan J. 2002 The conformational plasticity of protein kinases. Cell 109, 275-282. (doi:10.1016/S0092-8674(02)00741-9)
59. Johnson LN, Noble ME, Owen DJ. 1996 Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158. (doi:10.1016/S0092-8674(00) 81092-2)
60. Nolen B, Taylor S, Ghosh G. 2004 Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell. 15, 661-675. (doi:10.1016/j.molcel.2004.08.024)
61. Lowe ED, Noble ME, Skamnaki VT, Oikonomakos NG, Owen DJ, Johnson LN. 1997 The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition. EMBO J. 16, 6646-6658. (doi:10.1093/emboj/16.22. 6646)
62. Parang K, Till JH, Ablooglu AJ, Kohanski RA, Hubbard SR, Cole PA. 2001 Mechanism-based design of a protein kinase inhibitor. Nat. Struct. Biol. 8, 37-41. (doi:10.1038/83028)
63. Gibbs CS, Zoller MJ. 1991 Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions. J. Biol. Chem. 266, 8923-8931.
64. Schindler T, Bornmann W, Pellicena P, Miller WT, Clarkson B, Kuriyan J. 2000 Structural mechanism for STI-571 inhibition of abelson tyrosine kinase. Science 289, 1938-1942. (doi:10.1126/science.289.5486.1938)
65. Kornev AP, Haste NM, Taylor SS, Eyck LF. 2006 Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism. Proc. Natl Acad. Sci. USA 103, 17783-17788. (doi:10.1073/pnas.0607656103)
66. Dodson CA, Bayliss R. 2012 Activation of Aurora-A kinase by protein partner binding and phosphorylation are independent and synergistic. J. Biol. Chem. 287, 1150-1157. (doi:10.1074/jbc.M111.312090)
67. De Bondt HL, Rosenblatt J, Jancarik J, Jones HD, Morgan DO, Kim SH. 1993 Crystal structure of cyclin-dependent kinase 2. Nature 363, 595-602. (doi:10.1038/363595a0)
68. Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massague J, Pavletich NP. 1995 Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376, 313-320. (10.1038/376313a0)
69. Russo AA, Jeffrey PD, Pavletich NP. 1996 Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat. Struct. Biol. 3, 696-700. (doi:10.1038/nsb0896-696)
70. Wan PT et al. 2004 Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF. Cell 116, 855-867. (doi:10.1016/S0092- 8674(04)00215-6)
71. Xu W, Doshi A, Lei M, Eck MJ, Harrison SC. 1999 Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol. Cell. 3, 629-638. (doi:10.1016/S1097-2765(00)80356-1)
72. Nagar B, Hantschel O, Young MA, Scheffzek K, Veach D, Bornmann W, Clarkson B, Superti-Furga G, Kuriyan J. 2003 Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 112, 859-871. (doi:10.1016/S0092- 8674(03)00194-6)
73. Rellos P et al. 2007 Structure and regulation of the human Nek2 centrosomal kinase. J. Biol. Chem. 282, 6833-6842. (doi:10.1074/jbc.M609721200)
74. Westwood I, Cheary DM, Baxter JE, Richards MW, van Montfort RL, Fry AM, Bayliss R. 2009 Insights into the conformational variability and regulation of human Nek2 kinase. J. Mol. Biol. 386, 476-485. (doi:10.1016/j.jmb.2008.12.033)
75. Solanki S, Innocenti P, Mas-Droux C, Boxall K, Barillari C, van Montfort RL, Aherne GW, Bayliss R, Hoelder S. 2011 Benzimidazole inhibitors induce a DFG-out conformation of never in mitosis gene A-related kinase 2 (Nek2) without binding to the back pocket and reveal a nonlinear structure-activity relationship. J. Med. Chem. 54, 1626-1639. (doi:10.1021/jm1011726)
76. Whelligan DK et al. 2010 Aminopyrazine inhibitors binding to an unusual inactive conformation of the mitotic kinase Nek2: SAR and structural characterization. J. Med. Chem. 53, 7682-7698. (doi:10.1021/jm1008727)
77. Innocenti P et al. 2012 Design of potent and selective hybrid inhibitors of the mitotic kinase Nek2: structure-activity relationship, structural biology, and cellular activity. J. Med. Chem. 55, 3228-3241. (doi:10.1021/jm201683b)
78. Cheetham GM, Knegtel RM, Coll JT, Renwick SB, Swenson L, Weber P, Lippke JA, Austen DA. 2002 Crystal structure of aurora-2, an oncogenic serine/threonine kinase. J. Biol. Chem. 277, 42419-42422. (doi:10.1074/jbc.C200426200)
79. Dodson CA, Kosmopoulou M, Richards MW, Atrash B, Bavetsias V, Blagg J, Bayliss R. 2010 Crystal structure of an Aurora-A mutant that mimics Aurora-B bound to MLN8054: insights into selectivity and drug design. Biochem. J. 427, 19-28. (doi:10.1042/BJ20091530)
80. Heron NM et al. 2006 SAR and inhibitor complex structure determination of a novel class of potent and specific Aurora kinase inhibitors. Bioorg. Med. Chem. Lett. 16, 1320-1323. (doi:10.1016/j.bmcl.2005.11.053)
81. Bibby RA, Tang C, Faisal A, Drosopoulos K, Lubbe S, Houlston R, Bayliss R, Linardopoulos S. 2009 A cancer-associated aurora A mutant is mislocalized and misregulated due to loss of interaction with TPX2. J. Biol. Chem. 284, 33177-33184. (doi:10.1074/jbc.M109.032722)
82. Kang J, Yang M, Li B, Qi W, Zhang C, Shokat KM, Tomchick DR, Machius M, Yu H. 2008 Structure and substrate recruitment of the human spindle checkpoint kinase Bub1. Mol. Cell. 32, 394-405. (doi:10.1016/j.molcel.2008.09.017)
83. Littlepage LE, Wu H, Andresson T, Deaneham JK, Amundadottir LT, Ruderman JV. 2002 Identification of phosphorylated residues that affect the activity of the mitotic kinase Aurora-A. Proc. Natl Acad. Sci. USA 99, 15440-15445. (doi:10.1073/pnas.202606599)
84. Elling RA, Fucini RV, Romanowski MJ. 2008 Structures of the wild-type and activated catalytic domains of Brachydanio rerio Polo-like kinase 1 (Plk1): changes in the active-site conformation and interactions with ligands. Acta Crystallogr. D Biol. Crystallogr. 64, 909-918. (doi:10.1107/S0907444908019513)
85. Bayliss R, Sardon T, Vernos I, Conti E. 2003 Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol. Cell 12, 851-862. (doi:10.1016/S1097-2765(03)00392-7)
86. Sessa F, Mapelli M, Ciferri C, Tarricone C, Areces LB, Schneider TR, Stukenberg PT, Musacchio A. 2005 Mechanism of Aurora B activation by INCENP and inhibition by hesperadin. Mol. Cell 18, 379-391. (doi:10.1016/j.molcel.2005.03. 031)
87. Qian YW, Erikson E, Maller JL. 1998 Purification and cloning of a protein kinase that phosphorylates and activates the polo-like kinase Plx1. Science 282, 1701-1704. (doi:10.1126/science.282.5394.1701)
88. Ellinger-Ziegelbauer H, Karasuyama H, Yamada E, Tsujikawa K, Todokoro K, Nishida E. 2000 Ste20-like kinase (SLK), a regulatory kinase for polo-like kinase (Plk) during the G2/M transition in somatic cells. Genes Cells 5, 491-498. (doi:10.1046/j.1365-2443.2000.00337.x)
89. Kelm O, Wind M, Lehmann WD, Nigg EA. 2002 Cell cycle-regulated phosphorylation of the Xenopus polo-like kinase Plx1. J. Biol. Chem. 277, 25247-25256. (doi:10.1074/jbc.M202855200)
90. Scutt PJ, Chu ML, Sloane DA, Cherry M, Bignell CR, Williams DH, Eyers PA. 2009 Discovery and exploitation of inhibitor-resistant aurora and polo kinase mutants for the analysis of mitotic networks. J. Biol. Chem. 284, 15880-15893. (doi:10.1074/jbc.M109.005694)
91. Elia AE et al. 2003 The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain. Cell 115, 83-95. (doi:10.1016/S0092-8674(03)00725-6)
92. Cheng KY, Lowe ED, Sinclair J, Nigg EA, Johnson LN. 2003 The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex. EMBO J. 22, 5757-5768. (doi:10.1093/emboj/cdg558)
93. Yasui Y et al. 2004 Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis. J. Biol. Chem. 279, 12997-13003. (doi:10.1074/jbc.M311128200)
94. Jelluma N, Brenkman AB, van den Broek NJ, Cruijsen CW, van Osch MH, Lens SM, Medema RH, Kops GJ. 2008 Mps1 phosphorylates Borealin to control Aurora B activity and chromosome alignment. Cell 132, 233-246. (doi:10.1016/j.cell.2007. 11.046)
95. Plotnikova OV, Nikonova AS, Loskutov YV, Kozyulina PY, Pugacheva EN, Golemis EA. 2012 Calmodulin activation of Aurora-A kinase (AURKA) is required during ciliary disassembly and in mitosis. Mol. Biol. Cell. 23, 2658-2670. (doi:10.1091/mbc.E11-12-1056)
96. Reboutier D, Troadec MB, Cremet JY, Fukasawa K, Prigent C. 2012 Nucleophosmin/B23 activates Aurora A at the centrosome through phosphorylation of serine 89. J. Cell Biol. 197, 19-26. (doi:10.1083/jcb.201107134)
97. Zhang Y, Ni J, Huang Q, Ren W, Yu L, Zhao S. 2007 Identification of the auto-inhibitory domains of Aurora-A kinase. Biochem. Biophys. Res. Commun. 357, 347-352. (doi:10.1016/j.bbrc.2007.03.129)
98. Helps NR, Luo X, Barker HM, Cohen PT. 2000 NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1. Biochem. J. 349, 509-518. (doi:10.1042/0264-6021:3490509)
99. Mi J, Guo C, Brautigan DL, Larner JM. 2007 Protein phosphatase-1alpha regulates centrosome splitting through Nek2. Cancer Res. 67, 1082-1089. (doi:10.1158/0008-5472.CAN-06-3071)
100. Eto M, Elliott E, Prickett TD, Brautigan DL. 2002 Inhibitor-2 regulates protein phosphatase-1 complexed with NimA-related kinase to induce centrosome separation. J. Biol. Chem. 277, 44013-44020. (doi:10.1074/jbc.M208035200)
101. Mardin BR, Lange C, Baxter JE, Hardy T, Scholz SR, Fry AM, Schiebel E. 2010 Components of the Hippo pathway cooperate with Nek2 kinase to regulate centrosome disjunction. Nat. Cell. Biol. 12, 1166-1176. (doi:10.1038/ncb2120)
102. O'Regan L, Fry AM. 2009 The Nek6 and Nek7 protein kinases are required for robust mitotic spindle formation and cytokinesis. Mol. Cell. Biol. 29, 3975-3990. (doi:10.1128/MCB.01867-08)
103. Bertran MT, Sdelci S, Regue L, Avruch J, Caelles C, Roig J. 2011 Nek9 is a Plk1-activated kinase that controls early centrosome separation through Nek6/7 and Eg5. EMBO J. 30, 2634-2647. (doi:10.1038/emboj.2011.179)
104. Regue L, Sdelci S, Bertran MT, Caelles C, Reverter D, Roig J. 2011 DYNLL/LC8 protein controls signal transduction through the Nek9/Nek6 signaling module by regulating Nek6 binding to Nek9. J. Biol. Chem. 286, 18118-18129. (doi:10.1074/jbc.M110.209080)
105. Wang W et al. 2009 Structural and mechanistic insights into Mps1 kinase activation. J. Cell Mol. Med. 13, 1679-1694. (doi:10.1111/j.1582-4934.2008. 00605.x)
106. Kang J, Chen Y, Zhao Y, Yu H. 2007 Autophosphorylation-dependent activation of human Mps1 is required for the spindle checkpoint. Proc. Natl Acad. Sci. USA 104, 20232-20237. (doi:10.1073/pnas.0710519105)
107. Chu ML, Chavas LM, Douglas KT, Eyers PA, Tabernero L. 2008 Crystal structure of the catalytic domain of the mitotic checkpoint kinase Mps1 in complex with SP600125. J. Biol. Chem. 283, 21495-21500. (doi:10.1074/jbc. M803026200)
108. Chu ML et al. 2010 Biophysical and X-ray crystallographic analysis of Mps1 kinase inhibitor complexes. Biochemistry 49, 1689-1701. (doi:10.1021/bi901970c)
109. Kwiatkowski N et al. 2010 Small-molecule kinase inhibitors provide insight into Mps1 cell cycle function. Nat. Chem. Biol. 6, 359-368. (doi:10.1038/nchembio.345)
110. Heidebrecht HJ, Buck F, Steinmann J, Sprenger R, Wacker HH, Parwaresch R. 1997 p100: a novel proliferation-associated nuclear protein specifically restricted to cell cycle phases S, G2, and M. Blood 90, 226-233.
111. Earnshaw WC, Cooke CA. 1991 Analysis of the distribution of the INCENPs throughout mitosis reveals the existence of a pathway of structural changes in the chromosomes during metaphase and early events in cleavage furrow formation. J. Cell Sci. 98, 443-461.
112. Bayliss R, Sardon T, Ebert J, Lindner D, Vernos I, Conti E. 2004 Determinants for Aurora-A activation and Aurora-B discrimination by TPX2. Cell Cycle 3, 404-407. (doi:10.4161/cc.3.4.777)
113. Fu J, Bian M, Liu J, Jiang Q, Zhang C. 2009 A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function. Proc. Natl Acad. Sci. USA 106, 6939-6944. (doi:10.1073/pnas.0900833106)
114. Hans F, Skoufias DA, Dimitrov S, Margolis RL. 2009 Molecular distinctions between Aurora A and B: a single residue change transforms Aurora A into correctly localized and functional Aurora B. Mol. Biol. Cell 20, 3491-3502. (doi:10.1091/mbc.E09-05-0370)
115. Eswaran J, Patnaik D, Filippakopoulos P, Wang F, Stein RL, Murray JW, Higgins JM, Knapp S. 2009 Structure and functional characterization of the atypical human kinase haspin. Proc. Natl Acad. Sci. USA 106, 20198-20203. (doi:10.1073/pnas.0901989106)
116. Villa F, Capasso P, Tortorici M, Forneris F, de Marco A, Mattevi A, Musacchio A. 2009 Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. Proc. Natl Acad. Sci. USA 106, 20204-20209. (doi:10.1073/pnas.0908485106)
117. Olsen JV et al. 2010 Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. 3, ra3. (doi:10.1126/scisignal.2000475)
118. Zeng K, Bastos RN, Barr FA, Gruneberg U. 2010 Protein phosphatase 6 regulates mitotic spindle formation by controlling the T-loop phosphorylation state of Aurora A bound to its activator TPX2. J. Cell Biol. 191, 1315-1332. (doi:10.1083/jcb.201008106)
119. Gold MG, Barford D, Komander D. 2006 Lining the pockets of kinases and phosphatases. Curr. Opin. Struct. Biol. 16, 693-701. (doi:10.1016/j.sbi.2006.10. 006)
120. Alexander J et al. 2011 Spatial exclusivity combined with positive and negative selection of phosphorylation motifs is the basis for context-dependent mitotic signaling. Sci. Signal. 4, ra42. (doi:10.1126/scisignal.2001796)
121. Vaz Meirelles G, Ferreira Lanza DC, da Silva JC, Santana Bernachi J, Paes Leme AF, Kobarg J. 2010 Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome. J. Proteome Res. 9, 6298-6316. (doi:10.1021/pr100562w)
122. Bouloc N et al. 2010 Structure-based design of imidazo[1,2-a]pyrazine derivatives as selective inhibitors of Aurora-A kinase in cells. Bioorg. Med. Chem. Lett. 20, 5988-5993. (doi:10.1016/j.bmcl.2010.08.091)
123. Yan A, Wang L, Xu S, Xu J. 2011 Aurora-A kinase inhibitor scaffolds and binding modes. Drug Discov. Today 16, 260-269. (doi:10.1016/j.drudis.2010.12. 003)
124. Kothe M, Kohls D, Low S, Coli R, Rennie GR, Feru F, Kuhn C, Ding YH. 2007 Selectivity-determining residues in Plk1. Chem. Biol. Drug Des. 70, 540-546. (doi:10.1111/j.1747-0285.2007.00594.x)
125. Anderson K et al. 2007 Binding of TPX2 to Aurora A alters substrate and inhibitor interactions. Biochemistry 46, 10287-10295. (doi:10.1021/bi7011355)