Modulation of Wnt signaling by the nuclear localization of cellular FLIP-L

Journal of Cell Science

Volumn 123, Issue 1, 2010, Pages 23-28

  Katayama, Ryohei ^a,b   Ishioka, Toshiyasu ^a   Takada, Shinji ^c   Takada, Ritsuko ^c   Fujita, Naoya ^b   Tsuruo, Takashi ^b   Naito, Mikihiko ^a,d  

^a UNIVERSITY OF TOKYO   (Japan)

^b CANCER CHEMOTHERAPY CENTER   (Japan)

^c NATIONAL INSTITUTES OF NATURAL SCIENCES   (Japan)

^d NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

Author keywords

FLIP; NLS; Wnt signaling

Indexed keywords

BETA CATENIN; FLICE INHIBITORY PROTEIN; LEPTOMYCIN B; WNT PROTEIN;

APOPTOSIS; ARTICLE; CELL NUCLEUS; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOPLASM; GENE ACTIVITY; GENE DELETION; GENE EXPRESSION; GENE FUNCTION; GENE IDENTIFICATION; GENE INTERACTION; GENE LOCATION; GENE MUTATION; HUMAN; HUMAN CELL; NUCLEAR LOCALIZATION SIGNAL; PRIORITY JOURNAL;

ACTIVE TRANSPORT, CELL NUCLEUS; APOPTOSIS; CASP8 AND FADD-LIKE APOPTOSIS REGULATING PROTEIN; CELL LINE; CELL NUCLEUS; CLONING, MOLECULAR; CYTOPLASM; FATTY ACIDS, UNSATURATED; HUMANS; KARYOPHERINS; MUTANT PROTEINS; PROTEIN SORTING SIGNALS; PROTEIN TRANSPORT; RECEPTORS, CYTOPLASMIC AND NUCLEAR; SIGNAL TRANSDUCTION; WNT PROTEINS;

NES;

EID: 72449140675     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.058602     Document Type: Article

References (36)

1. Andersson, C. X., Fernandez-Rodriguez, J., Laos, S., Sikut, R., Sikut, A., Baeckstrom, D. and Hansson, G. C. (2004). CD43 has a functional NLS, interacts with beta-catenin, and affects gene expression. Biochem. Biophys. Res. Commun. 316, 12-17.
2. Chaudhary, P. M., Eby, M. T., Jasmin, A., Kumar, A., Liu, L. and Hood, L. (2000). Activation of the NF-kappaB pathway by caspase 8 and its homologs. Oncogene 19, 4451-4460.
3. Chung, J. H. and Eng, C. (2005). Nuclear-cytoplasmic partitioning of phosphatase and tensin homologue deleted on chromosome 10 (PTEN) differentially regulates the cell cycle and apoptosis. Cancer Res. 65, 8096-8100.
4. Clevers, H. (2006). Wnt/beta-catenin signaling in development and disease. Cell 127, 469-480.
5. Fang, L. W., Tai, T. S., Yu, W. N., Liao, F. and Lai, M. Z. (2004). Phosphatidylinositide 3-kinase priming couples c-FLIP to T cell activation. J. Biol. Chem. 279, 13-18.
6. Fasken, M. B., Saunders, R., Rosenberg, M. and Brighty, D. W. (2000). A leptomycin B-sensitive homologue of human CRM1 promotes nuclear export of nuclear export sequence-containing proteins in Drosophila cells. J. Biol. Chem. 275, 1878-1886.
7. Fischer, U., Huber, J., Boelens, W. C., Mattaj, I. W. and Luhrmann, R. (1995). The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82, 475-483.
8. Fornerod, M., Ohno, M., Yoshida, M. and Mattaj, I. W. (1997). CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90, 1051-1060.
9. Fukuda, M., Asano, S., Nakamura, T., Adachi, M., Yoshida, M., Yanagida, M. and Nishida, E. (1997). CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390, 308-311.
10. Gama-Carvalho, M. and Carmo-Fonseca, M. (2001). The rules and roles of nucleocytoplasmic shuttling proteins. FEBS Lett. 498, 157-163.
11. Gomez-Angelats, M. and Cidlowski, J. A. (2003). Molecular evidence for the nuclear localization of FADD. Cell Death Differ. 10, 791-797.
12. Harel, A. and Forbes, D. J. (2004). Importin beta: conducting a much larger cellular symphony. Mol. Cell 16, 319-330.
13. Hood, J. K. and Silver, P. A. (1999). In or out? Regulating nuclear transport. Curr. Opin. Cell Biol. 11, 241-247.
14. Irmler, M., Thome, M., Hahne, M., Schneider, P., Hofmann, K., Steiner, V., Bodmer, J. L., Schroter, M., Burns, K., Mattmann, C. et al. (1997). Inhibition of death receptor signals by cellular FLIP. Nature 388, 190-195.
15. Ishioka, T., Katayama, R., Kikuchi, R., Nishimoto, M., Takada, S., Takada, R., Matsuzawa, S., Reed, J. C., Tsuruo, T. and Naito, M. (2007). Impairment of the ubiquitin-proteasome system by cellular FLIP. Genes Cells 12, 735-744.
16. Kataoka, T. and Tschopp, J. (2004). N-terminal fragment of c-FLIP(L) processed by caspase 8 specifically interacts with TRAF2 and induces activation of the NF-kappaB signaling pathway. Mol. Cell. Biol. 24, 2627-2636.
17. Kataoka, T., Budd, R. C., Holler, N., Thome, M., Martinon, F., Irmler, M., Burns, K., Hahne, M., Kennedy, N., Kovacsovics, M. et al. (2000). The caspase-8 inhibitor FLIP promotes activation of NF-kappaB and Erk signaling pathways. Curr. Biol. 10, 640-648.
18. Korinek, V., Barker, N., Morin, P. J., van Wichen, D., de Weger, R., Kinzler, K. W., Vogelstein, B. and Clevers, H. (1997). Constitutive transcriptional activation by a beta-catenin-Tcf complex in APC-/- colon carcinoma. Science 275, 1784-1787.
19. Kudo, N., Wolff, B., Sekimoto, T., Schreiner, E. P., Yoneda, Y., Yanagida, M., Horinouchi, S. and Yoshida, M. (1998). Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1. Exp. Cell Res. 242, 540-547.
20. Kudo, N., Matsumori, N., Taoka, H., Fujiwara, D., Schreiner, E. P., Wolff, B., Yoshida, M. and Horinouchi, S. (1999). Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. Proc. Natl. Acad. Sci. USA 96, 9112-9117.
21. Lange, A., Mills, R. E., Lange, C. J., Stewart, M., Devine, S. E. and Corbett, A. H. (2007). Classical nuclear localization signals: definition, function, and interaction with importin alpha. J. Biol. Chem. 282, 5101-5105.
22. Logan, C. Y. and Nusse, R. (2004). The Wnt signaling pathway in development and disease. Annu. Rev. Cell Dev. Biol. 20, 781-810.
23. Mattaj, I. W. and Englmeier, L. (1998). Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67, 265-306.
24. Naito, M., Katayama, R., Ishioka, T., Suga, A., Takubo, K., Nanjo, M., Hashimoto, C., Taira, M., Takada, S., Takada, R. et al. (2004). Cellular FLIP inhibits beta-catenin ubiquitylation and enhances Wnt signaling. Mol. Cell. Biol. 24, 8418-8427.
25. Nakagiri, S., Murakami, A., Takada, S., Akiyama, T. and Yonehara, S. (2005). Viral FLIP enhances Wnt signaling downstream of stabilized beta-catenin, leading to control of cell growth. Mol. Cell. Biol. 25, 9249-9258.
26. Nakajima, A., Komazawa-Sakon, S., Takekawa, M., Sasazuki, T., Yeh, W. C., Yagita, H., Okumura, K. and Nakano, H. (2006). An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway. EMBO J. 25, 5549-5559.
27. Nigg, E. A. (1997). Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386, 779-787.
28. Qin, Z. H., Wang, Y., Kikly, K. K., Sapp, E., Kegel, K. B., Aronin, N. and DiFiglia, M. (2001). Pro-caspase-8 is predominantly localized in mitochondria and released into cytoplasm upon apoptotic stimulation. J. Biol. Chem. 276, 8079-8086.
29. Schickling, O., Stegh, A. H., Byrd, J. and Peter, M. E. (2001). Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription. Cell Death Differ. 8, 1157-1168.
30. Shibamoto, S., Higano, K., Takada, R., Ito, F., Takeichi, M. and Takada, S. (1998). Cytoskeletal reorganization by soluble Wnt-3a protein signalling. Genes Cells 3, 659-670.
31. Stade, K., Ford, C. S., Guthrie, C. and Weis, K. (1997). Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90, 1041-1050.
32. Wang, Y., Kakinuma, N., Zhu, Y. and Kiyama, R. (2006). Nucleo-cytoplasmic shuttling of human Kank protein accompanies intracellular translocation of beta-catenin. J. Cell Sci. 119, 4002-4010.
33. Weis, K. (1998). Importins and exportins: how to get in and out of the nucleus. Trends Biochem. Sci. 23, 185-189.
34. Wen, W., Meinkoth, J. L., Tsien, R. Y. and Taylor, S. S. (1995). Identification of a signal for rapid export of proteins from the nucleus. Cell 82, 463-473.
35. Wolff, B., Sanglier, J. J. and Wang, Y. (1997). Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem. Biol. 4, 139-147.
36. Zhan, Y., Hegde, R., Srinivasula, S. M., Fernandes-Alnemri, T. and Alnemri, E. S. (2002). Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC. Cell Death Differ. 9, 439-447.