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A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases

Shen, Shi-Hsiang, Bastien, Lison, Posner, Barry I., Chrétien, Pierre·1991·Nature
DOI 10.1038/352736a0
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Abstract

The phosphorylation of proteins at tyrosine residues is critical in cellular signal transduction, neoplastic transformation and control of the mitotic cycle. These mechanisms are regulated by the activities of both protein-tyrosine kinases (PTKs) and protein-tyrosine phosphatases (PTPases). As in the PTKs, there are two classes of PTPases: membrane associated, receptor-like enzymes and soluble proteins. Here we report the isolation of a complementary DNA clone encoding a new form of soluble PTPase, PTP1C. The enzyme possesses a large noncatalytic region at the N terminus which unexpectedly contains two adjacent copies of the Src homology region 2 (the SH2 domain) found in various nonreceptor PTKs and other cytoplasmic signalling proteins. As with other SH2 sequences, the SH2 domains of PTP1C formed high-affinity complexes with the activated epidermal growth factor receptor and other phosphotyrosine-containing proteins. These results suggest that the SH2 regions in PTP1C may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. PTPase activity may thus directly link growth factor receptors and other signalling proteins through protein-tyrosine phosphorylation.

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Research works printed but not linked: 30

  1. Jove, R. & Hanafusa, H. A. Rev. Cell Biol. 3, 31–56 (1987). · DOI
  2. Hanks, S. K., Quinn, A. M. & Hunter, T. Science 241, 42–52 (1988). · DOI
  3. Hunter, T. Cell 50, 823–829 (1987). · DOI
  4. Streuli, M., Krueger, N. X., Hall, L. R., Schlossman, S. F. & Saito, H. J. exp. Med. 168, 1523–1530 (1988). · DOI
  5. Krueger, N. X., Streuli, M. & Saito, H. EMBO J. 9, 3241–3252 (1990). · DOI
  6. Charbonneau, H. et al. Proc. natn. Acad. Sci. U.S.A. 86, 5252–5256 (1989). · DOI
  7. Cool, D. E. et al. Proc. natn. Acad. Sci. U.S.A. 86, 5257–5261 (1989). · DOI
  8. Sadowski, I. J. C., Stone, J. C. & Pawson, T. Molec. cell. Biol. 6, 4396–4408 (1986). · DOI
  9. Stahl, M. L., Ferenz, C. R., Kelleher, K. L., Kriz, R. W. & Knopf, J. L. Nature 332, 269–272 (1988). · DOI
  10. Moran, M. F. et al. Proc. natn. Acad. Sci. U.S.A. 87, 8622–8626 (1990). · DOI
  11. Mayer, B. J., Hamaguchi, M. & Hanafusa, H. Nature 332, 272–275 (1988). · DOI
  12. Engel, L. W. et al. Cancer Res. 38, 3352–3384 (1978).
  13. Studier, F. W., Rosenberg, A. H., Dunn, J. J. & Dubendorff, J. W. Meth. Enzym. 185, 60–89 (1990). · DOI
  14. Davis, S. et al. Science 252, 712–715 (1991). · DOI
  15. Koch, C. A., Anderson, D., Moran, M. F., Ellis, C. & Pawson, T. Science 252, 668–674 (1991). · DOI
  16. Escobedo, J. A. et al. Cell 65, 75–82 (1991). · DOI
  17. Mayer, B. J., Jackson, P. K. & Baltimore, D. Proc. natn. Acad. Sci. U.S.A. 88, 627–631 (1991). · DOI
  18. Matina, C. V. et al. Gene 74, 365–373 (1988). · DOI
  19. Fabricant R. N., De Larco, J. E. & Todaro, G. J. Proc. natn. Acad. Sci. U.S.A. 74, 565–569 (1987). · DOI
  20. Otsu, M. et al. Cell 65, 91–104 (1991). · DOI
  21. Marth, J. D., Peet, R., Krebs, E. G. & Perlmutter, R. M. Cell 43, 393–404 (1985). · DOI
  22. Zeigler, S. F., Martin, J. D., Lewis, D. B. & Perlmutter, R. M. Molec. cell. Biol. 7, 2276–2285 (1987). · DOI
  23. Cooke, M. P. & R. M. Perlmutter, R. M. New Biol. 1, 66–74 (1989).
  24. Simon, M. A., Drees, B., Kornberg, T. & Bishop, J. M. Cell 42, 831–840 (1985). · DOI
  25. Strebhardt, K., Mullins, J. I., Bruck, C. & Rübsamen-Waigmann, H. Proc. natn. Acad. Sci. U.S.A. 84, 8778–8782 (1987). · DOI
  26. Sukegawa, J. et al. Molec. cell. Biol. 7, 41–47 (1987). · DOI
  27. Fischman, K. et al. Molec. cell. Biol. 10, 146–153 (1986). · DOI
  28. Geryk, J. et al. J. Virol. 63, 481–492 (1989). · DOI
  29. Oppi, C., Shore, S. K. & Reddy, E. P. Proc. natn. Acad. Sci. U.S.A. 84, 8200–8204 (1987). · DOI
  30. Gregory, R. J., Kammermeyer, K. L., Vincent, W. S. III & Wadsworth, S. G. Molec. cell. Biol. 7, 2119–2127 (1987). · DOI

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Metadata

Authors
Shen, S.-H., Bastien, L., Posner, B. I., & Chrétien, P.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
1991-08-22
Volume
352
Issue
6337
Pages
736-739
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/352736a0
Cited by
295
References
0
Language
en
Update notices
correction (1991-10-31)
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