Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-α

Nature

Volumn 401, Issue 6753, 1999, Pages 606-610

  Jiang, Guoqiang ^a   Den Hertog, Jeroen ^b   Su, Jing ^c   Noel, Joseph ^a   Sap, Jan ^c   Hunter, Tony ^a  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^b HUBRECHT INSTITUTE   (Netherlands)

^c NEW YORK UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE PHOSPHATASE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVITY; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ANIMALIA;

EID: 0033533817     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/44170     Document Type: Article

References (28)

1. Hunter, T. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80, 225-236 (1995).
2. Tonks, N. K. & Neel, B. G. From form to function: signaling by protein tyrosine phosphatases. Cell 87, 365-368 (1996).
3. Bilwes, A. M., den Hertog, J., Hunter, T. & Noel, J. P. Structural basis for inhibition of receptor protein-tyrosine phosphatase α by dimerization. Nature 382, 555-559 (1996).
4. Weiss, A. & Schlessinger, J. Switching signals on or off by receptor dimerization. Cell 94, 277-280 (1998).
5. Desai, D. M., Sap, I., Schlessinger, J. & Weiss, A. Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell 73, 541-554 (1993).
6. Majeti, R., Bilwes, A. M., Noel, J. P., Hunter, T. & Weiss, A. Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge. Science 279, 88-91 (1998).
7. Felberg, J. & Johnson, P. Characterization of recombinant CD45 cytoplasmic domain proteins. Evidence for intramolecular and intermolecular interactions. J. Biol. Chem. 273, 17839-17845 (1998).
8. Wallace, M. J., Fladd, C., Batt, J. & Rotin, D. The second catalytic domain of protein tyrosine phosphatase δ (PTPδ) binds to and inhibits the first catalytic domain of PTPσ. Mol. Cell. Biol. 18, 2608-2616 (1998).
9. Sap, J., D'Eustachio, P., Givol, D. & Schlessinger, J. Cloning and expression of a widely expressed receptor tyrosine phosphatase. Proc. Natl Acad. Sci. USA 87, 6112-6116 (1990).
10. Wu, L., Buist, A., den Hertog, J. & Zhang, Z. Y. Comparative kinetic analysis and substrate specificity of the tandem catalytic domains of the receptor-like protein-tyrosine phosphatase α. J. Biol. Chem. 272, 6994-7002 (1997).
11. Harder, K. W., Moller, N. P., Peacock, J. W. & Jirik, F. R. Protein-tyrosine phosphatase α regulates Src family kinases and alters cell-substratum adhesion. J. Biol. Chem. 273, 31890-31900 (1998).
12. C-1PC and is involved in neuronal differentiation. EMBO J. 12, 3789-3798 (1993).
13. C-1PC by overexpression of a protein tyrosine phosphatase. Nature 359, 336-339 (1992).
14. Su, J., Muranjan, M. & Sap, J. Receptor protein tyrosine phosphatase α activates Src-family kinases and controls integrin-mediated responses in fibroblasts. Curr. Biol. 9, 505-511 (1999).
15. Ponniah, S., Wang, D. Z., Lim, K. L. & Pallen, C. J. Targeted disruption of the tyrosine phosphatase PTPα leads to constitutive downregulation of the kinases Src and Fyn. Curr. Biol. 9, 535-538 (1999).
16. neu+. J. Biol. Chem. 267, 20489-20492 (1992).
17. Burke, C. L. & Stern, D. F. Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface. Mol. Cell. Biol. 18, 5371-5379 (1998).
18. Sorokin, A., Lemmon, M. A., Ullrich, A. & Schlessinger, J. Stabilization of an active dimeric form of the epidermal growth factor receptor by introduction of an inter-receptor disulfide bond. J. Biol. Chem. 269, 9752-9759 (1994).
19. Kawakatsu, H. et al. A new monoclonal antibody which selectively recognizes the active form of Src tyrosine kinase. J. Biol. Chem. 271, 5680-5685 (1996).
20. Takeda, A., Wu, J. J. & Maizel, A. L. Evidence for monomeric and dimeric forms of CD45 associated with a 30-kDa phosphorylated protein. J. Biol. Chem. 267, 16651-16659 (1992).
21. Hoffmann, K. M., Tonks, N. K. & Barford, D. The crystal structure of domain 1 of receptor protein-tyrosine phosphatase μ. J. Biol. Chem. 272, 27505-27508 (1997).
22. Nam, H. J., Poy, F., Krueger, N. X., Saito, H. & Frederick, C. A. Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell 97, 449-457 (1999).
23. Tracy, S., van der Geer, P. & Hunter, T. The receptor-like protein-tyrosine phosphatase, RPTP α, is phosphorylated by protein kinase C on two serines close to the inner face of the plasma membrane. J. Biol. Chem. 270, 10587-10594 (1995).
24. den Hertog, J., Sap, J., Pals, C. E., Schlessinger, J. & Kruijer, W. Stimulation of receptor protein-tyrosine phosphatase a activity and phosphorylation by phorbol ester. Cell. Growth Differ. 6, 303-307 (1995).
25. den Hertog, J. & Hunter, T. Tight association of GRB2 with receptor protein-tyrosine phosphatase α is mediated by the SH2 and C-terminal SH3 domains. EMBO J. 15, 3016-3027 (1996).
26. Naviaux, R. K., Costanzi, E., Haas M. & Verma, I. M. The pCL vector system: rapid production of helper-free, high-titer, recombinant retroviruses. J. Virol. 70, 5701-5705 (1996).
27. Lipsich, L. A., Lewis, A. J. & Brugge, J. S. Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J. Virol. 48, 352-360 (1983).
28. Levy-Toledano, R., Caro, L. H., Hindman, N. & Taylor, S. I. Streptavidin blotting: a sensitive technique to study cell surface proteins; application to investigate autophosphorylation and endocytosis of biotin-labeled insulin receptors. Endocrinology 133, 1803-1808 (1993).