Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein

Nature

Volumn 397, Issue 6715, 1999, Pages 172-175

  Lopez Girona, Antonia ^a   Furnari, Beth ^a   Mondesert, Odile ^a   Russell, Paul ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; NUCLEAR PROTEIN; PROTEIN 14 3 3; PROTEIN CDC 25; PROTEIN RAD 24; UNCLASSIFIED DRUG;

ARTICLE; CELL CYCLE; CONTROLLED STUDY; DNA DAMAGE; DNA REPAIR; INTRACELLULAR TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; YEAST;

14-3-3 PROTEINS; BIOLOGICAL TRANSPORT; CARRIER PROTEINS; CDC2 PROTEIN KINASE; CELL CYCLE PROTEINS; CELL NUCLEUS; DNA DAMAGE; FUNGAL PROTEINS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; KARYOPHERINS; MUTAGENESIS; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; PROTEINS; RAS-GRF1; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECOMBINANT FUSION PROTEINS; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE PROTEINS; TYROSINE 3-MONOOXYGENASE; ULTRAVIOLET RAYS;

EID: 0033552943     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/16488     Document Type: Article

References (30)

1. Hartwell, L. H. & Weinert, T. A. Checkpoints: controls that ensure the order of cell cycle events. Science 246, 629-634 (1989)
2. Walworth, N., Davey, S. & Beach, D. Fission yeast chk1 protein kinase links the rad checkpoint pathway to cdc2. Nature 363, 368-371 (1993).
3. Rhind, N., Furnari, B. & Russell, P. Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast. Genes Dev. 11, 504-511 (1997).
4. Furnari, B., Rhind, N. & Russell, P. Cdc25 mitotic inducer targeted by Chk1 DNA damage checkpoint inase. Science 277, 1495-1497 (1997).
5. Sanchez, Y. et al. Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25. Science 277, 1497-1501 (1997).
6. Peng, C. Y. et al. Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216. Science 277, 1501 -1505 (1997).
7. Kumagai, A., Guo, Z., Emami, K. H., Wang, S. X. & Dunphy, W. G. The Xenopus Chk1 protein kinase mediates a caffeine-sensitive pathway of checkpoint control in cell-free extracts. J. Cell Biol. 142, 1559-1569 (1998).
8. Zeng, Y. et al. Replication checkpoint requires phosphorylation of the phosphatase Cdc25 by Cds1 or Chk1. Nature 395, 507-510 (1998).
9. Ford, J. C. et al 14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast. Science 265, 533-535 (1994).
10. Booher, R. N., Alfa, C. E., Hyams, J. S. & Beach, D. H. The fission yeast cdc2/cdc13/suc1 protein kinase: regulation of catalytic activity and nuclear localization. Cell 58, 485-497 (1989).
11. cdc25 mitotic inducer in fission yest. Nature 344, 549-552 (1990).
12. Muslin, A. J., Tanner, J. W., Allen, P. M. & Shaw, A. S. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84, 889-897 (1996).
13. Yaffe, M. B. et al The structural basis for 14-3-3: phosphopeptide binding specificity. Cell 91,961-971 (1997).
14. Peng, C. Y. et al. C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and promotes 14-3-3 protein binding. Cell Growth Differ. 9, 197-208 (1998).
15. Kumagai, A., Yakowec, P. S. & Dunphy, W. G. 14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts. Mol. Biol. Cell 9, 345-354 (1998).
16. Fornerod, M., Ohno, M., Yoshida, M. & Mattaj, I. W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90, 1051-1060 (1997).
17. Fukuda, M. et al. CRM1 responsible for intracellular transport mediated by the nuclear export signal. Nature 390, 308-310 (1997).
18. Ossareh-Nazari, B., Bachelerie, F. & Dargemont, C. Evidence for the role of Crm1 in signal-mediated nuclear protein export. Science 279, 141-144(1997).
19. Stade, K., Ford, C., Guthrie, C. & Weis, K. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90, 1041-1050 (1997).
20. Fischer, U., Huber, J., Boelens, W. C., Mattaj, I. W. & Luhrmann, R. The HlV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82, 475-483 (1995).
21. Fukuda, M., Gotoh, I., Gotoh,Y. & Nishida, E. Cytoplasmic localization of mitogen-activated protein kinase kinase directed by its NH2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal. J. Biol. Chem. 271, 20024-20028 (1996).
22. Gorlich, D. & Mattaj, I. W. Nucleocytoplasmic transport. Science 271, 1513-1518 (1996).
23. Suzuki, H., Nagai, K., Akutsu, E., Yamaki, H. & Tanaka, N. On the mechanism of action of bleomycin. Strand scission of DNA caused by bleomycin and its binding to DNA in vitro. J. Antibiot. 23, 473-480 (1970).
24. Kostrub, C. F., Knudsen, K., Suhramani, S. & Enoch, T. Huslp, a conserved fission yeast checkpoint protein, interacts with Radlp and is phosphorylated in response in DNA damage. EMBO J. 17, 2055-2066 (1998).
25. Dent, P., Jelinek, T., Morrison, D. K., Weber, M. J. & Sturgill, T. W. Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases. Science 268, 1902-1906 (1995).
26. Thorson, J. A. et al 14-3-3 proteins are required for maintenance of Raf-1 phosphorylation and kinase activity. Mol. Cell. Biol. 18, 5229-5238 (1998).
27. Moreno, S., Klar, A. & Nurse, P. Molecular genetic analysis of fission yeast Schizosaccharamyces pombe. Methods Enzymol. 194, 795-823 (1991).
28. Shiozaki, K, & Russell, P. Cell-cycle control linked to the extracellular environment by MAP kinase pathway in fission yeast. Nature 378, 739-743 (1995).
29. + that encodes a nuclear scaffold-like protein blocks spindle elongation in mitotic anaphase. J. Cell Biol. 106, 1171-1183 (1988).
30. Shiozaki, K. & Russell, P. S tress-activated protein kinase pathway in cell cycle control of fission yeast. Methods Enzymol. 283, 506-520 (1997).