Nuclear localization marker of FOXO3a: Can it be used to predict doxorubicin response?

Frontiers in Oncology

Volumn 3 JUN, Issue , 2013, Pages

  Gong, Chun ^a   Khoo, Ui Soon ^a  

^a UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

[No Author keywords available]

Indexed keywords

DOXORUBICIN; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR FKHRL1;

ANTINEOPLASTIC ACTIVITY; APOPTOSIS; CELL CYCLE REGULATION; CELL SURVIVAL; CYTOTOXICITY; DNA REPAIR; DRUG RESPONSE; HUMAN; NOTE; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; TISSUE MICROARRAY; UBIQUITINATION;

EID: 84891604445     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2013.00149     Document Type: Note

References (11)

1. Biggs, W. H., Meisenhelder, J., Hunter, T., Cavenee, W. K., and Arden, K. C. (1999). Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1. Proc. Natl. Acad. Sci. U.S.A. 96, 7421-7426. doi:10.1073/pnas.96.13.7421.
2. Chen, J., Gomes, A. R., Monteiro, L. J., Wong, S. Y., Wu, L. H., Ng, T. T., et al. (2010). Constitutively nuclear FOXO3a localization predicts poor survival and promotes Akt phosphorylation in breast cancer. PLoS ONE 5:e12293. doi:10.1371/journal.pone.0012293.
3. Gomes, A. R., Brosens, J. J., and Lam, E. W. (2008). Resist or die: FOXO transcription factors determine the cellular response to chemotherapy. Cell Cycle 7, 3133-3136. doi:10.4161/cc.7.20.6920.
4. Ho, K. K., McGuire, V. A., Koo, C. Y., Muir, K. W., de Olano, N., Maifoshie, E., et al. (2012). Phosphorylation of FOXO3a on Ser-7 by p38 promotes its nuclear localization in response to doxorubicin. J. Biol. Chem. 287, 1545-1555. doi:10.1074/jbc.M111.284224.
5. Hui, R. C., Francis, R. E., Guest, S. K., Costa, J. R., Gomes, A. R., Myatt, S. S., et al. (2008a). Doxorubicin activates FOXO3a to induce the expression of multidrug resistance gene ABCB1 (MDR1) in K562 leukemic cells. Mol. Cancer Ther. 7, 670-678. doi:10.1158/1535-7163.MCT-07-0397.
6. Hui, R. C., Gomes, A. R., Constantinidou, D., Costa, J. R., Karadedou, C. T., Fernandez de Mattos, S., et al. (2008b). The forkhead transcription factor FOXO3a increases phosphoinositide-3 kinase/Akt activity in drug-resistant leukemic cells through induction of PIK3CA expression. Mol. Cell. Biol. 28, 5886-5898. doi:10.1128/MCB.01265-07.
7. Paradis, S., and Ruvkun, G. (1998). Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor. Genes Dev. 12, 2488-2498. doi:10.1101/gad.12.16.2488.
8. Sunters, A., Madureira, P. A., Pomeranz, K. M., Aubert, M., Brosens, J. J., Cook, S. J., et al. (2006). Paclitaxel-induced nuclear translocation of FOXO3a in breast cancer cells is mediated by c-Jun NH2-terminal kinase and Akt. Cancer Res. 66, 212-220. doi:10.1158/0008-5472.CAN-05-1997.
9. Wilson, M. S., Brosens, J. J., Schwenen, H. D., and Lam, E. W. (2011). FOXO and FOXM1 in cancer: the FOXO-FOXM1 axis shapes the outcome of cancer chemotherapy. Curr. Drug Targets 12, 1256-1266. doi:10.2174/138945011796150244.
10. Yang, J. Y., and Hung, M. C. (2009). A new fork for clinical application: targeting forkhead transcription factors in cancer. Clin. Cancer Res. 15, 752-757. doi:10.1158/1078-0432.CCR-08-0124.
11. Yang, J. Y., Zong, C. S., Xia, W., Yamaguchi, H., Ding, Q., Xie, X., et al. (2008). ERK promotes tumorigenesis by inhibiting FOXO3a via MDM2-mediated degradation. Nat. Cell Biol. 10, 138-148. doi:10.1038/ncb1676.