A Structural Rationale for Selective Stabilization of Anti-tumor Interactions of 14-3-3 proteins by Cotylenin A

Journal of Molecular Biology

Volumn 386, Issue 4, 2009, Pages 913-919

  Ottmann, Christian ^a,b   Weyand, Michael ^a   Sassa, Takeshi ^c   Inoue, Takatsugu ^d   Kato, Nobuo ^d   Wittinghofer, Alfred ^e   Oecking, Claudia ^b  

^a CHEMICAL GENOMICS CENTRE OF THE MAX PLANCK SOCIETY   (Germany)

^b UNIVERSITY OF TÜBINGEN   (Germany)

^c YAMAGATA UNIVERSITY   (Japan)

^d OSAKA UNIVERSITY   (Japan)

^e MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

differentiation therapy; natural compound; protein protein stabilization; X ray

Indexed keywords

CARBON; COTYLENIN A; DITERPENE; DITERPENOID; FUNGAL PROTEIN; FUSICOCCIN; PROTEIN 14 3 3; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; HYDROXYLATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; STRUCTURE ANALYSIS;

EID: 60149087610     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.01.005     Document Type: Article

References (34)

1. Tenen D.G. Disruption of differentiation in human cancer: AML shows the way. Nature Rev. Cancer 3 (2003) 89-101
2. Asahi K., Honma Y., Hazeki K., Sassa T., Kubohara Y., Sakurai A., and Takahashi N. Cotylenin A, a plant-growth regulator, induces the differentiation in murine and human myeloid leukemia cells. Biochem. Biophys. Res. Commun. 238 (1997) 758-763
3. Yamada K., Honma Y., Asahi K.I., Sassa T., Hino K.I., and Tomoyasu S. Differentiation of human acute myeloid leukaemia cells in primary culture in response to cotylenin A, a plant growth regulator. Brit. J. Haem. 114 (2001) 814-821
4. Honma Y., Ishii Y., Sassa T., and Asahi K. Treatment of human promyelocytic leukemia in the SCID mouse model with cotylenin A, an inducer of myelomonocytic differentiation of leukemia cells. Leuk. Res. 27 (2003) 1019-1025
5. Kasukabe T., Okabe-Kado J., Kato N., Sassa T., and Honma Y. Antitumor effect of cotylenin A plus interferon-alpha: possible therapeutic agents against ovary carcinoma. Breast Canc. Res. 7 (2005) 1097-1110
6. Honma Y., Ishii Y., Yamamoto-Yamaguchi Y., Sassa T., and Asahi K. Cotylenin A, a differentiation-inducing agent, and IFN-alpha cooperatively induce apoptosis and have an antitumor effect on human non-small cell lung carcinoma cells in nude mice. Cancer Res. 63 (2003) 3659-3666
7. Honma Y., Kasukabe T., Yamori T., Kato N., and Sassa T. Antitumor effect of cotylenin A plus interferon-alpha: possible therapeutic agents against ovary carcinoma. Gyn. Onc. 99 (2005) 680-688
8. Sassa T., Tojyo T., and Munakata K. Isolation of a new plant growth substance with cytokinin-like activity. Nature 227 (1970) 379-381
9. Ballio A., Chain E.B., De Leo P., Erlanger B.F., Mauri M., and Tonolo A. Fusicoccin: a new wilting toxin produced by Fusicoccum amygdali Del. Nature 203 (1964) 297
10. Tzivion G., Gupta V.S., Kaplun L., and Balan V. 14-3-3 proteins as potential oncogenes. Semin. Cancer Biol. 16 (2006) 203-213
11. Jin J., Smith F.D., Stark C., Wells C.D., Fawcett J.P., Kulkarni S., et al. Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Curr. Biol. 14 (2004) 1436-1450
12. Benzinger A., Muster N., Koch H.B., Yates III J.R., and Hermeking H. Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. Mol. Cell. Proteomics 4 (2005) 785-795
13. Pozuelo-Rubio M., Geraghty K.M., Wong B.H., Wood N.T., Campbell D.G., Morrice N., and Mackintosh C. 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking. Biochem. J. 379 (2004) 395-408
14. Meek S.E., Lane W.S., and Piwnica-Worms H. Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. J. Biol. Chem. 279 (2004) 32046-32054
15. Fantl W.J., Muslin A.J., Kikuchi A., Martin J.A., MacNicol A.M., Gross R.W., and Williams L.T. Activation of Raf-1 by 14-3-3 proteins. Nature 371 (1994) 612-614
16. Freed E., Symons M., Macdonald S.G., McCormick F., and Ruggieri R. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265 (1994) 1713-1716
17. Conklin D.S., Galaktinov K., and Beach D. 14-3-3 Proteins associate with cdc25 phosphatases. Proc. Natl Acad. Sci. USA 92 (1995) 7892-7896
18. Peng C.Y., Graves P.R., Thoma R.S., Wu Z., Shaw A.S., and Piwnica-Worms H. Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of cdc25C on serine-216. Science 277 (1997) 1497-1501
19. O'Kelly I., Butler M.H., Zilberberg N., and Goldstein S. Forward transport: 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111 (2002) 577-588
20. Hermeking H. The 14-3-3 cancer connection. Nature Rev. Cancer 3 (2003) 931-943
21. Berg D., Holzmann C., and Riess O. 14-3-3 proteins in the nervous system. Nat. Rev. Neurosci. 9 (2003) 752-762
22. Fu H., Coburn J., and Collier R.J. The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family. Proc. Natl Acad. Sci. USA 90 (1993) 2320-2324
23. Ottmann C., Yasmin L., Weyand M., Veesenmeyer J.L., Diaz M.H., Palmer R.H., et al. Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. EMBO J. 26 (2007) 902-913
24. Rittinger K., Budman J., Xu J., Volinia S., Cantley L.C., Smerdon S.J., et al. Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol. Cell 4 (1999) 153-166
25. Ganguly S., Weller J.L., Ho A., Chemineau P., Malpaux B., and Klein D.C. Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205. Proc. Natl Acad. Sci. USA 102 (2005) 1222-1227
26. Jahn T., Fuglsang A.T., Olsson A., Brüntrup I.M., Collinge D.B., Volkmann D., et al. The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H+-ATPase. Plant Cell 9 (1997) 1805-1814
27. Oecking C., Piotrowski M., Hagemeier J., and Hagemann K. Topology and target interaction of the fusicoccin-binding 14-3-3 homologs of Commelina communis. Plant J. 12 (1997) 441-453
28. Wuertele M., Jelich-Ottmann C., Wittinghofer A., and Oecking C. Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J. 22 (2003) 987-994
29. +-ATPase by combining X-ray crystallography and electron cryomicroscopy. Mol. Cell 25 (2007) 427-440
30. Wanzel M., Kleine-Kohlbrecher D., Herold S., Hock A., Berns K., Park J., et al. Akt and 14-3-3η regulate Miz1 to control cell-cycle arrest after DNA damage. Nature Cell Biol. 7 (2005) 30-41
31. Tajima N., Nukina M., Kato N., and Sassa T. Novel fusicoccins R and S, and the fusicoccin S aglycon (phomopsiol) from Phomopsis amygdali niigata 2-A, and their seed germination-stimulating activity in the presence of abscisic acid. Biosci. Biotechnol. Biochem. 68 (2004) 1125-1130
32. Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
33. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
34. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132