Constitutive STAT1 tyrosine phosphorylation in U937 monocytes overexpressing the TYK2 protein tyrosine kinase does not induce gene transcription

Cell Growth and Differentiation

Volumn 7, Issue 6, 1996, Pages 833-840

  Eilers, Andreas ^a   Kanda, Kayoko ^a   Klose, Birgit ^a   Krolewski, John ^b   Decker, Thomas ^a  

^a Institute of Microbiology and Genetics Vienna   (Austria)

^b The New York Presbyterian Hospital   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTERFERON; INTERFERON RECEPTOR; PROTEIN TYROSINE KINASE; TRANSCRIPTION FACTOR;

ARTICLE; CELLULAR DISTRIBUTION; ENZYME ACTIVATION; GENE EXPRESSION; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; MONOCYTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; TRANSGENE;

CELL DIFFERENTIATION; CELL LINE; DNA-BINDING PROTEINS; ENZYME ACTIVATION; GENETIC ENGINEERING; HUMANS; JANUS KINASE 1; MONOCYTES; PHOSPHORYLATION; PROTEIN BIOSYNTHESIS; PROTEIN-TYROSINE KINASES; PROTEINS; STAT1 TRANSCRIPTION FACTOR; STEM CELLS; SUBCELLULAR FRACTIONS; TRANS-ACTIVATORS; TRANSCRIPTION, GENETIC; TRANSGENES; TYK2 KINASE;

JANUS; STAPHYLOCOCCUS PHAGE 3A;

EID: 0029827828     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (48)

1. Damell, J. E., Jr., Kerr, I. M., and Stark, G. R. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science (Washington DC), 264: 1415-1421, 1994.
2. Ihle, J. E., and Kerr, I. M. Jaks and Stats in signaling by the cytokine receptor superfamily. Trends Genet., 11: 69-74, 1995.
3. De Maeyer, E., and De Maeyer-Guignard, J. Interferons and Other Regulatory Cytokines. New York: John Wiley & Sons, Inc., 1988.
4. Pfeffer, L. M., and Constantinescu, S-N. The molecular biology of IFN-β, from receptor binding to transmembrane signaling. In: A. T. Reder (ed.), Interferon Therapy of Multiple Sclerosis. New York: Marcel Dekker, Inc., in press, 1996.
5. Uze, G., Lutfalla, G., and Mogensen, K. E. IFN-α and -β and their receptors and their friends and relations. J. Interferon Cytokine Res., 15: 3-26, 1995.
6. Colamonichi, O. R., D'Alessandro, F., Diaz, M. O., Gregory, S. A., Neckers, L. M., and Nordan, R. Characterization of three monoclonal antibodies that recognize the IFN-α2 receptor. Proc. Natl. Acad Sci. USA, 87: 7230-7234, 1990.
7. Abramovich, C., Shulman, L. M., Ratovitski, E., Harroch, S., Tovey, M., Eid, P., and Revel, M. Differential tyrosine phosphorylation of the IFNAR chain of the type I IFN receptor and of an associated surface protein in response to IFN-α and IFN-β. EMBO J., 13: 5871-5877, 1994.
8. tyk2, an IFN-α-activated tyrosine kinase, is physically associated with an IFN-α receptor. J. Biol. Chem., 269: 3518-3522, 1994.
9. tyk2 tyrosine kinase. Mol. Cell. Biol., 14: 8133-8124, 1994.
10. Novick, D., Coden, B., and Rubinstein, M. The human IFN-α/β receptor: characterization and molecular cloning. Cell, 77: 391-400, 1994.
11. Velazquez, L., Fellous, M., Stark, G. R., and Pellegrini, S. A protein tyrosine kinase in the IFN-α/β signaling pathway. Cell, 70: 313-322, 1992.
12. Domanski, P., Witte, M. M., Kellum, M., Rubinstein, M., Hackett, R., Pitha, P., and Colamonici, O. Cloning and expression of a long form of the β subunit of the IFN-α/β receptor that is required for signaling. J. Biol. Chem., 270: 21606-21611, 1995.
13. Lutfalla, G., Holland, S. J., Cinato, E., Monneron, D., Reboul, J., Rogers, N. C., Smith, J. M., Stark, G. R., Gardiner, K., Mogensen, K. E., Kerr, I. M., and Uze, G. Mutant U5A cells are complemented by an IFN-α/β receptor subunit generated by alternative processing of a new member of a cytokine receptor gene cluster. EMBO J., 14: 5100-5108, 1995.
14. Decker, T. The molecular biology of type I interferons: gene activation, promoters, proteins induced. In: A. T. Reder (ed.), Interferon Therapy of Multiple Sclerosis. New York: Marcel Dekker, Inc., in press, 1996.
15. Decker, T., Lew, D. J., and Darnell, J. E., Jr. Two distinct IFN-α-dependent signal transduction pathways may contribute to activation of transcription of the GBP gene. Mol. Cell. Biol., 11: 5147-5153, 1991.
16. Seegert, D. S., Strehlow, I., Klose, B., Levy, D. E., Schindler, C., and Decker, T. A novel, IFN-α-regulated, DNA-binding protein participates in the regulation of the IFP53/tryptophanyl-tRNA synthetase gene. J. Biol. Chem., 269: 8590-8595, 1994.
17. Müller, M., Briscoe, J., Laxton, C., Guschin, D., Zimiecki, A., Silvennoinen, O., Harpur, A. G., Barbieri, G., Wirthuhn, B. A., Schindler, C., Pellegrini, S., Wilks, A., Ihle, J. N., Stark, G. R., and Kerr, I. M. The protein tyrosine kinase jakl complements defects in IFN-α/β and -γ signal transduction. Nature (Lond.), 366: 129-135, 1993.
18. Walling, D., Guschin, D., Müller, M., Silvennoinen, O., Witthuhn, B. A., Quelle, F. W., Rogers, N. C., Schindler, C., Stark, G. R., Ihle, J. N., and Kerr, I. M. Complementation by the protein tyrosine kinase jak2 of a mutant cell line defective in the IFN-γ signal transduction pathway. Nature (Lond.), 356: 166-170, 1993.
19. Sakatsume, M., Igarashi, K-I., Winestock, K. D., Garotta, G., Larner, A. C., and Finbloom, D. S. The Jak kinases differentially associate with the α and β (accessory factor) chains of the IFN-γ receptor to form a functional receptor unit capable of activating STAT transcription factors. J. Biol. Chem., 270: 17528-17534, 1995.
20. Briscoe, J., Rogers, N. C., Witthuhn, B. A., Watling, D., Harpur, A. G., Wilks, A. F., Stark, G. R., Ihle, J. N., and Kerr, I. Kinase negative mutants of JAK1 can sustain IFN-γ-inducible gene expression but not an antiviral state. EMBO J., 15: 799-809, 1996.
21. Improta, T., Schindler, C., Horvath, C. M., Kerr, I. M., Stark, G. R., and Darnell, J. E., Jr. Transcription factor ISGF-3 formation requires phosphorylated Stat 91 protein, but Stat 113 protein is phosphorylated independently of Stat 91 protein. Proc. Natl. Acad. Sci. USA, 91: 4776-4780, 1994.
22. Leung, S., Qureshi, S. A., Kerr, I. M., Darnell, J. E., and Stark, G. R. Role of STAT2 in the IFN-α signaling pathway. Mol. Cell. Biol., 15: 1312-1317, 1995.
23. Van, H., Greenland, A., Gupta, S., Lim, T., Schreiber, R., Schindler, C., and Krolewski, J. J. Phosphorylated IFN-α receptor 1 subunit (IFNαR1) acts as a docking site for the latent form of the 113-kDa STAT2 protein. EMBO J.,175: 1064-1074, 1996.
24. Greenlund, A. C., Farrar, M. A., Viviano, B. L., and Schreiber, R. D. Ligand-induced IFN-γ receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91). EMBO J., 13: 1591-1600, 1994.
25. Greenlund, A. C., Morales, M. O., Viviano, B. L., Van, H., Krolewski, J., and Schreiber, R. D. Stat recruitment by tyrosine-phosphorylated cytokine receptors: an ordered reversible affinity-driven process. Immunity, 2: 677-687, 1995.
26. Heim, M. H., Kerr, I. M., Stark, G. R., and Darnell, J. E. Contributions of STAT SH2 groups to specific IFN signaling by the Jak-STAT pathway. Science (Washington DC), 267: 1347-1349, 1995.
27. Quells, F. W., Thierfelder, W., Witthuhn, B. A., Tang, B., Cohen, S., and Ihle, J. N. Phosphorylation and activation of the DNA binding activity of purified STAT1 by the Janus protein-tyrosine kinases and the epidermal growth factor receptor. J. Biol. Chem., 270: 20775-20780, 1995.
28. Chun-Fai, L., Ripperger, J., Morella, K. K., Wang, Y., Gearing, D. P., Horseman, N. D., Campos, S. P., Fey, G. H., and Baumann, H. STAT3 and STAT5B are targets of two different signal pathways activated by hematopoietin receptors and control transcription via separate cytokine response elements. J. Biol. Chem., 270: 23254-23257, 1995.
29. Damen, J. E., Wakao, H., Miyajima, A., Krosl, J., Humphries, R. K., Cutler, R. L., and Krystal, G. Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation. EMBO J., 14: 5557-5568, 1995.
30. Silvennoinen, O., Ihle, J. N., Schlessinger, J., and Levy, D. E. IFN-induced nuclear signalling by Jak protein tyrosine kinases. Nature (Lond.), 366: 583-585, 1993.
31. Chang, Y. N., Jeang, K. T., Chiou, C. J., Chan, Y. J., Pizzorno, M., and Hayward, G. S. Identification of a large bent DNA domain and binding sites for serum response factor adjacent to the NF1 repeat cluster and enhancer region in the major IE94 promoter from simian cylomegalovirus. J. Virol., 67: 516-529, 1993.
32. Eilers, A., Georgellis, D., Klose, B., Schindler, C., Zimiecki, A., Harpur, A. G., Wilks, A. F., and Decker, T. Differentiation-regulated serine phosptiorylation of STAT 1 promotes GAP activation in macrophages. Mol. Cell. Biol., 15: 3579-3586, 1995.
33. Barbieri, G., Velasquez, L. Scrobogna, M., Fellous, M., and Pellegrini, S. Activation of the protein tyrosine kinase tyk2 by IFN-α/β. Eur. J. Biochem., 223: 427-435, 1994.
34. Pine, R., Canova, A., and Schindler, C. Tyrosine phosphorylated p91 binds to a single element in the ISGF2/IRF-1 promoter to mediate induction by IFN-α and IFN-γ and is likely to autoregulate the p91 gene. EMBO J., 13: 158-167, 1994.
35. Strehlow, I., Seegert, D., Frick, C., Bange, F-C., Schindler, C., Boettger, E. C., and Decker, T. The gene encoding IFP 53/tryptophanyl-tRNA synthetase is regulated by the γ-INF activation factor. J. Biol. Chem., 268: 16590-16595, 1993.
36. Colamonichi, O. R., Pfeffer, L. M., D'Alessandro, F., Platanias, L. C., Gregory, S. A., Rosolen, A., Nordan, R., Cruciani, R. A., and Diaz, M. O. Multichain structure of the IFN-α receptor on hematopoietic cells. J. Immunol., 148: 2126-2132, 1992.
37. Colamonici, O., Domanski, P., Krolewski, J., Fu, X-Y., Reich, N., Pfeffer, L. M., Sweet, M. E., and Platanias, L. C. Interferon α (IFN-α) signaling in cells expressing the variant form of the type IIFN receptor. J. Biol. Chem., 269: 5660-5665, 1994.
38. Constantinescu, S. N., Croze, E., Murti, A., Wang, C., Basu, L., Hollander, D., Russell-Harde, D., Betts, M., Garcia-Martinez, V., Mullersman, J. E., and Pfeffer, L. M. Expression and signaling specificity of the IFNAR chain of the type I IFN receptor complex. Proc. Natl. Acad. Sci. USA, 92: 10487-10491, 1995.
39. Wen, Z., Zhong, Z., and Darnell, J. E., Jr. Maximal activation of transcription by Stall and Stat3 requires both tyrosine and serine phosphorylaton. Cell, 82: 241-250, 1995.
40. David, M., Petricoin, E. F., III, Benjamin, C., Pine, R., Weber, M. J., and Lamer, A. C. Requirement for MAP kinase (ERK2) activity in interferon-α and interferon-β-stimulated gene expression through STAT proteins. Science (Washington DC), 269: 1721-1723, 1995.
41. Schindler, C., Fu, X-Y., Improta, T., Aebersold, R. H., and Darnell, J. E. The proteins of ISGF-3: one gene encodes 91- and 84-kDa ISGF-3α proteins. Proc. Natl. Acad. Sci. USA, 89: 7836-7839, 1992.
42. Fu, X-Y., Schindler, C., Improta, T., Aebersold, R. H., and Darnell, J. E., Jr. The proteins of ISGF-3, the IFN-α induced activator, define a new gene family of signal transducers. Proc. Natl. Acad Sci. USA, 89: 7840-7843, 1992.
43. Wilks, A. F., Harpur, A., Kurban, R. R., Ralph, S. J., Zurcher, G., and Zimiecki, A. Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase. Mol. Cell. Biol., 11: 2057-2065, 1991
44. Eilers, A., Seegert, D., Schindler, C., Baccarini, M., and Decker, T. The response of the γ IFN activation factor (GAF) is under developmental control in cells of the macrophage lineage. Mol. Cell. Biol., 13: 3245-3254, 1993.
45. Eilers, A., Baccarini, M., Horn, F., Hipskind, R. A., Schindler, C., and Decker, T. A factor induced by differentiating signals in cells of the macrophage lineage binds to the γ IFN activation site. Mol. Cell. Biol., 14: 1364-1373, 1994.
46. Reich, N. C., Evans, B., Levy, D. E., Fahey, D. E., Knight, E., and Darnell, J. E. IFN-induced transcription of a gene encoding a 15-kDa protein depends on an upstream enhancer element. Proc. Natl. Acad. Sci. USA, 84: 6394-6398, 1987.
47. Chomczynski, P., and Sacchi N. Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem., 162: 156-161, 1987.
48. Sambrook, J., Fritsch, E. F., and Maniatis, T. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1989.