Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis

Science

Volumn 330, Issue 6011, 2010, Pages 1670-1673

  Mochida, Satoru ^a,b   Maslen, Sarah L ^a   Skehel, Mark ^a   Hunt, Tim ^a  

^a IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

^b KUMAMOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ENDOSULFINE; CYCLIN DEPENDENT KINASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN KINASE; PROTEIN KINASE GREATWALL; SULFUR DERIVATIVE; UNCLASSIFIED DRUG;

DEVELOPMENTAL BIOLOGY; EGG; ENZYME ACTIVITY; EUKARYOTE; INHIBITION; INHIBITOR; PROTEIN;

ARTICLE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; INTERPHASE; MITOSIS; NONHUMAN; PRIORITY JOURNAL; XENOPUS;

ANIMALS; CDC2 PROTEIN KINASE; CELL CYCLE; INTERPHASE; MITOSIS; MUTANT PROTEINS; OOCYTES; PEPTIDES; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN PHOSPHATASE 2; PROTEIN-SERINE-THREONINE KINASES; SERINE; XENOPUS LAEVIS; XENOPUS PROTEINS;

EUKARYOTA;

EID: 78650366525     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1195689     Document Type: Article

References (31)

1. D. O. Morgan, in The Cell Cycle: Principles of Control (Primers in Biology) (New Science Press, London, 2007), p. 297.
2. A. Lindqvist, V. Rodríguez-Bravo, R. H. Medema, J. Cell Biol. 185, 193 (2009).
3. A. Kumagai, W. G. Dunphy, Cell 70, 139 (1992).
4. P. R. Mueller, T. R. Coleman, W. G. Dunphy, Mol. Biol. Cell 6, 119 (1995).
5. S. Y. Kim, E. J. Song, K. J. Lee, J. E. Ferrell Jr., Mol. Cell. Biol. 25, 10580 (2005).
6. S. L. Harvey, A. Charlet, W. Haas, S. P. Gygi, D. R. Kellogg, Cell 122, 407 (2005).
7. G. Pal, M. T. Paraz, D. R. Kellogg, J. Cell Biol. 180, 931 (2008).
8. S. Mochida, S. Ikeo, J. Gannon, T. Hunt, EMBO J. 28, 2777 (2009).
9. P. V. Castilho, B. C. Williams, S. Mochida, Y. Zhao, M. L. Goldberg, Mol. Biol. Cell 20, 4777 (2009).
10. S. Mochida, T. Hunt, Nature 449, 336 (2007).
11. J. Yu, Y. Zhao, Z. Li, S. Galas, M. L. Goldberg, Mol. Cell 22, 83 (2006).
12. S. Vigneron et al., EMBO J. 28, 2786 (2009).
13. M. Goldberg, personal communication.
14. P. Cohen, A. Knebel, Biochem. J. 393, 1 (2006).
15. Methods are available as supporting material on Science Online.
16. J. A. Girault, A. Horiuchi, E. L. Gustafson, N. L. Rosen, P. Greengard, J. Neurosci. 10, 1124 (1990).
17. A. Virsolvy-Vergine et al., Proc. Natl. Acad. Sci. U.S.A. 89, 6629 (1992).
18. L. Gros et al., Diabetologia 45, 703 (2002).
19. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
20. I. Dulubova et al., J. Neurochem. 77, 229 (2001).
21. E. Kinoshita, E. Kinoshita-Kikuta, K. Takiyama, T. Koike, Mol. Cell. Proteomics 5, 749 (2006).
22. A. W. Murray, Cell Biol. 36, 581 (1991).
23. K. Ohsumi, T. M. Yamamoto, M. Iwabuchi, Methods Mol. Biol. 322, 445 (2006).
24. G. Goshima et al., Science 316, 417 (2007); 10.1126/science.1141314.
25. J. R. Von Stetina et al., Development 135, 3697 (2008).
26. D. Drummond-Barbosa, A. C. Spradling, Dev. Biol. 266, 310 (2004).
27. A. Burgess et al., Proc. Natl. Acad. Sci. U.S.A. 107, 12564 (2010).
28. S. Mangan, A. Zaslaver, U. Alon, J. Mol. Biol. 334, 197 (2003).
29. K. Ishii, K. Kumada, T. Toda, M. Yanagida, EMBO J. 15, 6629 (1996).
30. J. Q. Wu et al., Nat. Cell Biol. 11, 644 (2009).
31. 15 of Cdk1 (CP 3.2). S.M. was supported by a fellowship from the Japan Society for the Promotion of Science.