Perinuclear localization of the protein-tyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells

European Journal of Cell Biology

Volumn 79, Issue 4, 2000, Pages 261-271

  Tenev, Tencho ^a,b   Böhmer, Sylvia Annette ^b   Kaufmann, Roland ^b   Frese, Steffen ^b   Bittorf, Thomas ^c   Beckers, Thomas ^d   Böhmer, Frank D ^b  

^a IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

^c UNIVERSITY OF ROSTOCK   (Germany)

^d ASTA MEDICA AG   (Germany)

Author keywords

Epidermal growth factor receptor; Localization; Protein tyrosine phosphatase; Regulatable expression system; SHP 1; Signal transducer and activator of transcription

Indexed keywords

CALCIMYCIN; EPIDERMAL GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE PHOSPHATASE; STAT1 PROTEIN; STAT3 PROTEIN;

ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; CELL NUCLEUS; CONTROLLED STUDY; ENZYME LOCALIZATION; EXPRESSION VECTOR; GENE INDUCTION; KERATINOCYTE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING;

ANIMALIA;

EID: 0343729328     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1078/S0171-9335(04)70029-1     Document Type: Article

References (42)

1. Adachi, M., Fischer, E. H., Ihle, J., Imai, K., Jirik, F., Neel, B., Pawson, T., Shen, S. H., Thomas, M., Ullrich, A., Zhao, Z. Z. (1996): Mammalian SH2-containing protein-tyrosine phosphatases. Cell 85, 15.
2. Andrews, N. C., Faller, D. V. (1991): A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian cells. Nucleic Acids Res. 19, 2499.
3. Baasner, S., Melchner, H. von, Klenner, T., Hilgard, P., Beckers, T. (1996): Reversible tumorigenesis in mice by conditional expression of the HER2/c-erbB2 receptor tyrosine kinase. Oncogene 13, 901-911.
4. Banville, D., Stocco, R., Shen, S. H. (1995): Human protein tyrosine phosphatase 1c (ptpn6) gene structure - alternate promoter usage and exon skipping generate multiple transcripts. Genomics 27, 165-173.
5. Bittorf, T., Jaster, R., Ludtke, B., Kamper, B., Brock, J. (1997): Requirement for JAK2 in erythropoietin-induced signalling pathways. Cell. Signalling 9, 85-89.
6. Böhmer, F. D., Böhmer, A., Heldin, C. H. (1993): The dephosphorylation characteristics of the receptors for epidermal growth factor and platelet-derived growth factor in Swiss 3T3-cell membranes suggest differential regulation of receptor signalling by endogenous protein-tyrosine phosphatases. FEBS Lett. 331, 276-280.
7. Böhmer, F. D., Böhmer, A., Obermeier, A., Ullrich, A. (1995): Use of selective tyrosine kinase blockers to monitor growth factor receptor dephosphorylation in intact cells. Anal. Biochem. 228, 267-273.
8. Brumell, J. H., Chan, C. K., Butler, J., Borregaard, N., Siminovitch, K. A., Grinstein, S., Downey, G. P. (1997): Regulation of src homology 2-containing tyrosine phosphatase-1 during activation of human neutrophils - role of protein kinase C. J. Biol. Chem. 272, 875-882.
9. Chen, C., Okayama, H. (1987): High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7, 2745-2752.
10. Chen, H. E., Chang, S., Trub, T., Neel, B. G. (1996): Regulation of colony-stimulating factor-1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SH-PTP1. Mol. Cell. Biol. 16, 3685-3697.
11. David, M., Chen, H. E., Goelz, S., Larner, A. C., Neel, B. G. (1995): Differential regulation of the alpha/beta interferon-stimulated Jak/ Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 15, 7050-7058.
12. Dayton, M. A., Knobloch, T. J. (1997): Multiple phosphotyrosine phosphatase messenger-RNAs are expressed in the human lung fibroblast cell line wi-38. Rec. Signal Transd. 7, 241-256.
13. Faure, R., Baquiran, G., Bergeron, J. J. M., Posner, B. I. (1992): The dephosphorylation of insulin and epidermal growth factor receptors. Role of endosome-associated phosphotyrosine phosphatases. J. Biol. Chem. 267, 11215-11221.
14. Feng, G. S., Pawson, T. (1994): Phosphotyrosine phosphatases with SH2 domains - regulators of signal transduction. Trends Genet. 10, 54-58.
15. Flint, A. J., Tiganis, T., Barford, D., Tonks, N. K. (1997): Development of substrate-trapping mutants to identify physiological substrates of protein-tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 94, 1680-1685.
16. Görlich, D., Rapoport, T. A. (1993): Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75, 615-630.
17. Gossen, M., Bujard, H. (1992): Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA 89, 5547-5551.
18. Gossen, M., Bonin, A. L., Freundlieb, S., Bujard, H. (1994): Inducible gene expression systems for higher eukaryotic cells. Curr. Opin. Biotechnol. 5, 516-520.
19. Graham, J. M. (1997): Homogenization of tissues and cells. In: J. M. Graham, D. Rickwood (eds.): Subcellular Fractionation. A Practical Approach, Oxford University Press, Oxford, New York, Tokyo, pp. 1-29.
20. Hofmann, A., Nolan, G. P., Blau, H. M. (1996): Rapid retroviral delivery of tetracycline-inducible genes in a single autoregulatory cassette. Proc. Natl. Acad. Sci. USA 93, 5185-5190.
21. Iwamoto, Y., Chin, Y. E., Peng, X. B., Fu, X. Y. (1998): Identification of a membrane-associated inhibitor(s) of epidermal growth factor-induced signal transducer and activator of transcription activation. J. Biol. Chem. 273, 18198-18204.
22. Keilhack, H., Tenev, T., Nyakatura, E., Godovac-Zimmermann. J., Nielsen, L., Seedorf, K., Böhmer, F. D. (1998): Phosphotyrosine-1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling. J. Biol. Chem. 273, 24839-24846.
23. Klingmüller, U., Lorenz, U., Cantley, L. C., Neel, B. G., Lodish, H. F. (1995): Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80, 729-738.
24. Lammers, R., Bossenmaier, B., Cool, D. E., Tonks, N. K., Schlessinger, J., Fischer, E. H., Ullrich, A. (1993): Differential activities of protein tyrosine phosphatases in intact cells. J. Biol. Chem. 268, 22456-22462.
25. Leach, K. L., Powers, E. A., Ruff, V. A., Jaken, S., Kaufmann, S. (1989): Type 3 protein kinase C localization to the nuclear envelope of phorbol ester-treated NIH 3T3 cells. J. Cell Biol. 109, 685-695.
26. Li, R. Y., Gaits, F., Ragab, A., Ragab-Thomas, J. M. F., Chap, H. (1994): Translocation of an SH2-containing protein tyrosine phosphatase (SH-PTP1) to the cytoskeleton of thrombin-activated platelets. FEBS Lett. 343, 89-93.
27. Lorenz, U., Bergemann, A. D., Steinberg, H. N., Flanagan, J. G., Li, X., Galli, S. J., Neel, B.C. (1996): Genetic analysis reveals cell type-specific regulation of receptor tyrosine kinase c-Kit by the protein tyrosine phosphatase SHP-1. J. Exp. Med. 184, 1111-1126.
28. Neel, B. G., Tonks, N. K. (1997): Protein-tyrosine phosphatases in signal transduction. Curr. Opin. Cell Biol. 9, 193-204.
29. Paulson, R. F., Vesely, S., Siminovitch, K. A., Bernstein, A. (1996): Signaling by the w/kit receptor tyrosine kinase is negatively regulated in vivo by the protein-tyrosine phosphatase SHP-1. Nature Genetics 13, 309-315.
30. Ram, P. A., Waxman, D. J. (1997): Interaction of growth hormone-activated STATs with SH2-containing phosphotyrosine phosphatase SHP-1 and nuclear JAK2 tyrosine kinase. J. Biol. Chem. 272, 17694-17702.
31. Rickwood, D., Messent, A., Patel, D. (1997): Isolation and characterization of nuclei and nuclear subfractions. In: J. M. Graham, D. Rickwood (eds.): Subcellular Fractionation. A Practical Approach, Oxford University Press, Oxford, New York, Tokyo, pp. 71-105.
32. Schaapveld, R., Wieringa, B., Hendriks, W. (1997): Receptor-like protein-tyrosine phosphatases - alike and yet so different. Mol. Biol. Rep. 24, 247-262.
33. Suarez Pestana, E., Tenev, T., Groß, S., Ogata, M., Böhmer, F. D. (1999): The transmembrane protein-tyrosine phosphatase RPTPσ modulates signaling of the epidermal growth factor receptor in A431 cells. Oncogene 18, 4069-4079.
34. Sweizer, T. D., Hanover, J. A. (1996): Calmodulin activates nuclear protein import: A link between signal transduction and nuclear transport. Proc. Natl. Acad. Sci. USA 93, 14574-14579.
35. Tenev, T., Keilhack, H., Tomic, S., Stoyanov, B., Steingerlach, M., Lammers, R., Krivtsov, A. V., Ullrich, A., Böhmer, F. D. (1997): Both SH2 domains are involved in interaction of SHP-1 with the epidermal growth factor receptor but cannot confer receptor-directed activity to SHP-1/SHP-2 chimera. J. Biol. Chem. 272, 5966-5973.
36. Tomic, S., Greiser, U., Lammers, R., Kharitonenkov, A., Imyanitov, E., Ullrich, A., Böhmer, F.D. (1995): Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTPIC. J. Biol. Chem. 270, 21277-21284.
37. Tonks, N. K., Neel, B. G. (1996): From form to function: signaling by protein tyrosine phosphatases. Cell 87, 365-368.
38. Vogel, W., Lammers, R., Huang, J., Ullrich, A. (1993): Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation. Science 259, 1611-1614.
39. Yi, T. L., Mui, A. L. F., Krystal, G., Ihle, J. N. (1993): Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor-beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis. Mol. Cell. Biol. 13, 7577-7586.
40. You, M., Zhao, Z. Z. (1997): Positive effects of SH2 domain-containing tyrosine phosphatase SHP-1 on epidermal growth factor-stimulated and interferon-gamma-stimulated activation of STAT transcription factors in HeLa cells. J. Biol. Chem. 272, 23376-23381.
41. Zhao, Z. H., Shen, S. H., Fischer, E. H. (1994): Phorbol ester-induced expression, phosphorylation, and translocation of protein-tyrosine phosphatase 1C in HL-60cells. Proc. Natl. Acad. Sci. USA 91, 5007-5011.
42. Zhong, Z., Wen, Z., Darnell, J. J. (1994): Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6. Science 264, 95-98.