Aurora-A phosphorylates augmin complex component hice1 protein at an N-terminal serine/threonine cluster to modulate its microtubule binding activity during spindle assembly

Journal of Biological Chemistry

Volumn 286, Issue 34, 2011, Pages 30097-30106

  Tsai, Connie Y ^a   Ngo, Bryan ^a   Tapadia, Anjali ^a   Hsu, Pang Hung ^b   Wu, Guikai ^a   Lee, Wen Hwa ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b NATIONAL TAIWAN OCEAN UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ACTIVITIES; BIPOLAR SPINDLES; COMPLEX COMPONENTS; IMMUNOSTAINING; IN-VITRO; IN-VIVO; MICROTUBULE NUCLEATION; MICROTUBULES; MINIMAL EFFECTS; MITOTIC PROGRESSION; MITOTIC REGULATORS; MITOTIC SPINDLE; N-TERMINALS; SPINDLE POLE; SPINDLE-ASSEMBLY;

ENZYMES; NUCLEATION; PHOSPHORYLATION; POLES;

AMINO ACIDS;

AUGMIN COMPLEX; AURORA A KINASE; CELL CYCLE PROTEIN; MULTIPROTEIN COMPLEX; MUTANT PROTEIN; PROTEIN FAM29A; PROTEIN HICE1; SERINE; THREONINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANAPHASE; ARTICLE; CHROMOSOME SEGREGATION; CONTROLLED STUDY; ENZYME BINDING; ENZYME REGULATION; GENE CLUSTER; HUMAN; HUMAN CELL; IMMUNOHISTOCHEMISTRY; IN VITRO STUDY; METAPHASE; MICROTUBULE ASSEMBLY; MITOSIS; MITOSIS SPINDLE; OSTEOSARCOMA CELL; POINT MUTATION; PRIORITY JOURNAL; PROPHASE; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; SPINDLE POLE BODY;

CELL LINE, TUMOR; HUMANS; METAPHASE; MICROTUBULE-ASSOCIATED PROTEINS; MICROTUBULES; MITOTIC SPINDLE APPARATUS; MUTATION; PHOSPHORYLATION; PROPHASE; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES;

EID: 80051929486     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.266767     Document Type: Article

References (40)

1. Gadde, S., and Heald, R. (2004) Curr. Biol. 14, R797-R805
2. Kline-Smith, S. L., and Walczak, C. E. (2004) Mol. Cell 15, 317-327
3. O'Connell, C. B., and Khodjakov, A. L. (2007) J. Cell Sci. 120, 1717-1722
4. Heald, R., and Walczak, C. E. (2009) in The Kinetochore, pp 1-38, Springer, New York
5. Lüders, J., and Stearns, T. (2007) Nat. Rev. Mol. Cell Biol. 8, 161-167
6. Wiese, C., and Zheng, Y. (2006) J. Cell Sci. 119, 4143-4153
7. Gruss, O. J., and Vernos, I. (2004) J. Cell Biol. 166, 949-955
8. Heald, R., Tournebize, R., Blank, T., Sandaltzopoulos, R., Becker, P., Hyman, A., and Karsenti, E. (1996) Nature 382, 420-425
9. Kaláb, P., Pralle, A., Isacoff, E. Y., Heald, R., and Weis, K. (2006) Nature 440, 697-701
10. Kalab, P., and Heald, R. (2008) J. Cell Sci. 121, 1577-1586
11. Kalab, P., Weis, K., and Heald, R. (2002) Science 295, 2452-2456
12. Goshima, G., and Kimura, A. (2010) Curr. Opin. Cell Biol. 22, 44-49
13. Goshima, G., Mayer, M., Zhang, N., Stuurman, N., and Vale, R. D. (2008) J. Cell Biol. 181, 421-429
14. Lawo, S., Bashkurov, M., Mullin, M., Ferreria, M. G., Kittler, R., Habermann, B., Tagliaferro, A., Poser, I., Hutchins, J. R., Hegemann, B., Pinchev, D., Buchholz, F., Peters, J. M., Hyman, A. A., Gingras, A. C., and Pelletier, L. (2009) Curr. Biol. 19, 816-826
15. Meireles, A. M., Fisher, K. H., Colombié, N., Wakefield, J. G., and Ohkura, H. (2009) J. Cell Biol. 184, 777-784
16. Uehara, R., Nozawa, R. S., Tomioka, A., Petry, S., Vale, R. D., Obuse, C., and Goshima, G. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 6998-7003
17. Wainman, A., Buster, D. W., Duncan, T., Metz, J., Ma, A., Sharp, D., and Wakefield, J. G. (2009) Genes Dev. 23, 1876-1881
18. Zhu, H., Coppinger, J. A., Jang, C. Y., Yates, J. R., 3rd, and Fang, G. (2008) J. Cell Biol. 183, 835-848
19. Zhu, H., Fang, K., and Fang, G. (2009) Mol. Cells 27, 1-3
20. Wu, G., Lin, Y. T., Wei, R., Chen, Y., Shan, Z., and Lee, W. H. (2008) Mol. Cell. Biol. 28, 3652-3662
21. Wu, G., Wei, R., Cheng, E., Ngo, B., and Lee, W. H. (2009) Mol. Biol. Cell 20, 4686-4695
22. Marumoto, T., Zhang, D., and Saya, H. (2005) Nat. Rev. Cancer 5, 42-50
23. Barr, A. R., and Gergely, F. (2007) J. Cell Sci. 120, 2987-2996
24. Glover, D. M., Leibowitz, M. H., McLean, D. A., and Parry, H. (1995) Cell 81, 95-105
25. Roghi, C., Giet, R., Uzbekov, R., Morin, N., Chartrain, I., Le Guellec, R., Couturier, A., Dorée, M., Philippe, M., and Prigent, C. (1998) J. Cell Sci.111, 557-572
26. Hannak, E., Kirkham, M., Hyman, A. A., and Oegema, K. (2001) J. Cell Biol. 155, 1109-1116
27. Liu, Q., and Ruderman, J. V. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 5811-5816
28. Cowley, D. O., Rivera-Pérez, J. A., Schliekelman, M., He, Y. J., Oliver, T. G., Lu, L., O'Quinn, R., Salmon, E. D., Magnuson, T., and Van Dyke, T. (2009) Mol. Cell. Biol. 29, 1059-1071
29. Harrington, E. A., Bebbington, D., Moore, J., Rasmussen, R. K., Ajose-Adeogun, A. O., Nakayama, T., Graham, J. A., Demur, C., Hercend, T., Diu-Hercend, A., Su, M., Golec, J. M., and Miller, K. M. (2004) Nat. Med. 10, 262-267
30. Arlot-Bonnemains, Y., Klotzbucher, A., Giet, R., Uzbekov, R., Bihan, R., and Prigent, C. (2001) FEBS Lett. 508, 149-152
31. Floyd, S., Pines, J., and Lindon, C. (2008) Curr. Biol. 18, 1649-1658
32. Littlepage, L. E., and Ruderman, J. V. (2002) Genes Dev. 16, 2274-2285
33. Taguchi, S., Honda, K., Sugiura, K., Yamaguchi, A., Furukawa, K., and Urano, T. (2002) FEBS Lett. 519, 59-65
34. Kim, Y., Holland, A. J., Lan, W., and Cleveland, D. W. (2010) Cell 142, 444-455
35. Katayama, H., Zhou, H., Li, Q., Tatsuka, M., and Sen, S. (2001) J. Biol. Chem. 276, 46219-46224
36. Illenberger, S., Drewes, G., Trinczek, B., Biernat, J., Meyer, H. E., Olmsted, J. B., Mandelkow, E. M., and Mandelkow, E. (1996) J. Biol. Chem. 271, 10834-10843
37. Jang, C. Y., Coppinger, J. A., Seki, A., Yates, J. R., 3rd, and Fang, G. (2009) J. Cell Sci. 122, 1334-1341
38. Jang, C. Y., Coppinger, J. A., Yates, J. R., 3rd, and Fang, G. (2011) Biochem. Biophys. Res. Commun. 408, 174-179
39. Romé, P., Montembault, E., Franck, N., Pascal, A., Glover, D. M., and Giet, R. g. (2010) J. Cell Biol. 189, 651-659
40. Rong, R., Jiang, L. Y., Sheikh, M. S., and Huang, Y. (2007) Oncogene 26, 7700-7708