Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway

Science

Volumn 278, Issue 5343, 1997, Pages 1638-1641

  Chow, Chi Wing ^a   Rincón, Mercedes ^b   Cavanagh, Julie ^a   Dickens, Martin ^a   Davis, Roger J ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF VERMONT COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; ARTICLE; CELL STIMULATION; DEPHOSPHORYLATION; IMMUNE RESPONSE; IMMUNOPRECIPITATION; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION;

ANIMALS; BINDING SITES; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CALCINEURIN; CELL LINE; CELL NUCLEUS; COS CELLS; CYCLOSPORINE; CYTOPLASM; DNA-BINDING PROTEINS; HUMANS; JNK MITOGEN-ACTIVATED PROTEIN KINASES; JURKAT CELLS; MITOGEN-ACTIVATED PROTEIN KINASE KINASES; MITOGEN-ACTIVATED PROTEIN KINASES; MUTATION; NFATC TRANSCRIPTION FACTORS; NUCLEAR PROTEINS; PHOSPHORYLATION; PROTEIN KINASES; RECOMBINANT FUSION PROTEINS; SIGNAL TRANSDUCTION; T-LYMPHOCYTES; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

EID: 0030706186     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.278.5343.1638     Document Type: Article

References (31)

1. B. Dérijard et al., Cell 76, 1025 (1994); J. M. Kyriakis et al., Nature 369, 156 (1994).
2. B. Dérijard et al., Cell 76, 1025 (1994); J. M. Kyriakis et al., Nature 369, 156 (1994).
3. A. J. Whitmarsh and R. J. Davis, J. Mol. Med. 74, 589 (1996).
4. H. K. Sluss, Z. Han, T. Barrett, R. J. Davis, T. Ip, Genes Dev. 10, 2745 (1996); J. R. Riesgo-Escovar, M. Jenni, A. Fritz, E. Hafen, ibid., p. 2759.
5. H. K. Sluss, Z. Han, T. Barrett, R. J. Davis, T. Ip, Genes Dev. 10, 2745 (1996); J. R. Riesgo-Escovar, M. Jenni, A. Fritz, E. Hafen, ibid., p. 2759.
6. 6 transformants) of a mouse embryo cDNA library was done with the yeast strain L40 [Z. Galcheva-Gargova et al., Science 272, 1797 (1996)]. The bait plasmid (pLexA-JNK1) was constructed by insertion of JNK1 in the polylinker of pBTM116 [M. Dickens et al., ibid. 277, 693 (1997)].
7. 6 transformants) of a mouse embryo cDNA library was done with the yeast strain L40 [Z. Galcheva-Gargova et al., Science 272, 1797 (1996)]. The bait plasmid (pLexA-JNK1) was constructed by insertion of JNK1 in the polylinker of pBTM116 [M. Dickens et al., ibid. 277, 693 (1997)].
8. T. Hoey, Y.-L. Sun, K. Williamson, X. Xu, Immunity 2, 461 (1995).
9. S. N. Ho, D. J. Thomas, L. A. Timmerman, U. Franke, G. R. Crabtree, J. Biol. Chem. 270, 19898 (1995); E. S. Masuda et al., Mol. Cell. Biol. 15, 2697 (1995).
10. S. N. Ho, D. J. Thomas, L. A. Timmerman, U. Franke, G. R. Crabtree, J. Biol. Chem. 270, 19898 (1995); E. S. Masuda et al., Mol. Cell. Biol. 15, 2697 (1995).
11. S. L. Schreiber and G. R. Crabtree, Immunol. Today 13, 136 (1992); G. R. Crabtree and N. A. Clipstone, Annu. Rev. Biochem. 63, 1045 (1994); A. Rao, Immunol. Today 15, 274 (1994); J. Leukocyte Biol. 57, 536 (1995).
12. S. L. Schreiber and G. R. Crabtree, Immunol. Today 13, 136 (1992); G. R. Crabtree and N. A. Clipstone, Annu. Rev. Biochem. 63, 1045 (1994); A. Rao, Immunol. Today 15, 274 (1994); J. Leukocyte Biol. 57, 536 (1995).
13. S. L. Schreiber and G. R. Crabtree, Immunol. Today 13, 136 (1992); G. R. Crabtree and N. A. Clipstone, Annu. Rev. Biochem. 63, 1045 (1994); A. Rao, Immunol. Today 15, 274 (1994); J. Leukocyte Biol. 57, 536 (1995).
14. S. L. Schreiber and G. R. Crabtree, Immunol. Today 13, 136 (1992); G. R. Crabtree and N. A. Clipstone, Annu. Rev. Biochem. 63, 1045 (1994); A. Rao, Immunol. Today 15, 274 (1994); J. Leukocyte Biol. 57, 536 (1995).
15. J. Raingeaud et al., J. Biol. Chem. 270, 7420 (1995).
16. B. Su et al., Cell 77, 727 (1994).
17. C.-W. Chow and J. Cavanagh, unpublished data.
18. C. R. Beals, N. A. Clipstone, S. N. Ho, G. R. Crabtree, Genes Dev. 11, 824 (1997); C. R. Beals, C. M. Sheridan, C. W. Turck, P. Gardner, G. R. Crabtree, Science 275, 1930 (1997).
19. C. R. Beals, N. A. Clipstone, S. N. Ho, G. R. Crabtree, Genes Dev. 11, 824 (1997); C. R. Beals, C. M. Sheridan, C. W. Turck, P. Gardner, G. R. Crabtree, Science 275, 1930 (1997).
20. S. Gupta, D. Campbell, B. Dérijard, R. J. Davis, Science 267, 389 (1995).
21. F. Shibasaki, E. R. Price, D. Lian, F. McKeon, Nature 382, 370 (1996).
22. C. Tournier, A. J. Whitmarsh, J. Cavanagh, T. Barrett, R. J. Davis, Proc. Natl. Acad. Sci. U.S.A. 94, 7337 (1997).
23. D. Yang et al., ibid., p. 3004.
24. D. Cantrell, Annu. Rev. Immunol. 14, 259 (1996); E. Genot, S. Cleverly, S. Henning, D. Cantrell, EMBO J. 15, 3923 (1996).
25. D. Cantrell, Annu. Rev. Immunol. 14, 259 (1996); E. Genot, S. Cleverly, S. Henning, D. Cantrell, EMBO J. 15, 3923 (1996).
26. S. Gupta et al., EMBO J. 15, 2760 (1996).
27. Expression vectors for activated calcineurin [Y. Watanabe, B. A. Perrino, B. H. Chang, T. R. Soderling, J. Biol. Chem. 270, 456 (1995)], JNK (77), MKK7 (14), Ras61L (7), and dominant negative c-Jun [TAM67(A3-122)] [U. R. Rapp, J. Troppmair, T. Beck, M. J. Birrer, Oncogene 9, 3493 (1994)] have been described. The human NFAT3 and NFAT4 cD-NAs were cloned in the polylinker of the expression vector pCDNA3 (Invitrogen). The human NFATc and NFATp cDNAs cloned in the vector pREP4 were obtained from T. Hoey (5). The polymerase chain reaction (PCR) was used to create mutations. GAL4 and glutathione-S-transferase (GST) fusion proteins were constructed by subcloning PCR fragments in the polylinker of pSG424 and pGEX-5X-1 (17).
28. Expression vectors for activated calcineurin [Y. Watanabe, B. A. Perrino, B. H. Chang, T. R. Soderling, J. Biol. Chem. 270, 456 (1995)], JNK (77), MKK7 (14), Ras61L (7), and dominant negative c-Jun [TAM67(A3-122)] [U. R. Rapp, J. Troppmair, T. Beck, M. J. Birrer, Oncogene 9, 3493 (1994)] have been described. The human NFAT3 and NFAT4 cD-NAs were cloned in the polylinker of the expression vector pCDNA3 (Invitrogen). The human NFATc and NFATp cDNAs cloned in the vector pREP4 were obtained from T. Hoey (5). The polymerase chain reaction (PCR) was used to create mutations. GAL4 and glutathione-S-transferase (GST) fusion proteins were constructed by subcloning PCR fragments in the polylinker of pSG424 and pGEX-5X-1 (17).
29. Electroporation (Jurkat T cells) and lipofectamine (COS-1 and BHK cells) were used for transfection studies (Gibco-BRL). Luciferase reporter gene expression was examined in cotransfection assays. The IL-2 NFAT (5) and GAL4 (77) luciferase reporter plasmids have been described. Transfection efficiency was monitored with a β-galactosidase expression vector. Luciferase and β-galactosidase activities were measured in cell lysates 48 hours after transfection (17). The data are presented as the relative luciferase activity [mean ± SD (n = 3) of the luciferase/β-galactosidase activity ratio].
30. BHK cells were grown on poly-D-lysine-coated cover slips, fixed with 4% paraformaldehyde, permeabilized with 0.25% Triton X-100, and processed for immunofluorescence microscopy. The primary antibody used for epitope-tagged proteins was the mouse monoclonal antibody (mAb) M2 (IBI-Kodak). NFATc and NFATp were detected by means of a mAb (Affinity Bioreagents) and a rabbit polycional antibody (Upstate Biotechnology), respectively. The secondary antibodies were Texas Red-labeled goat antibody to mouse immunoglobulin (Ig) and rhodamine-labeled goat antibody to rabbit Ig (Jackson Immunoresearch).
31. We thank M. Birrer, J. Cooper, T. Hoey, S. Hollenberg, and T. Soderling for reagents; S. Doxsey for assistance with microscopy; T. Barrett for DNA sequencing; and K. Gemme for secretarial assistance. Supported in part by National Cancer Institute grants CA58396 and CA65831. R.J.D. is an Investigator of the Howard Hughes Medical Institute.