Tyrosine phosphorylation of transmembrane ligands for Eph receptors

Science

Volumn 275, Issue 5306, 1997, Pages 1640-1643

  Brückner, Katja ^a   Pasquale, Elena B ^b   Klein, Rüdiger ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b BURNHAM INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE; TYROSINE;

ARTICLE; CELL COMMUNICATION; EMBRYO DEVELOPMENT; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION;

3T3 CELLS; ANIMALS; AXONS; BRAIN-DERIVED NEUROTROPHIC FACTOR; CELL MEMBRANE; EMBRYO; EPHRIN-B1; LIGANDS; MICE; PHOSPHORYLATION; PHOSPHOTYROSINE; PLATELET-DERIVED GROWTH FACTOR; PROTEINS; RECEPTOR PROTEIN-TYROSINE KINASES; RECEPTOR, CILIARY NEUROTROPHIC FACTOR; RECEPTOR, EPHB2; RECEPTORS, NERVE GROWTH FACTOR; RECEPTORS, PLATELET-DERIVED GROWTH FACTOR; RECOMBINANT FUSION PROTEINS; SIGNAL TRANSDUCTION; TRANSFECTION;

EID: 0030891962     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.275.5306.1640     Document Type: Article

References (38)

1. S. Davis et al., Science 266, 816 (1994).
2. R. Brambilla et al., EMBO J. 14, 3116 (1995).
3. R. Brambilla and R. Klein, Mol. Cell. Neurosci. 6, 487 (1995).
4. N. W. Gale et al., Neuron 17, 9 (1996).
5. U. Drescher et al., Cell 82, 359 (1995).
6. H.-J. Cheng, M. Nakamoto, A. D. Bergemann, J. G. Flanagan, ibid., p. 371.
7. Q. Xu, G. Alldus, R. Macdonald, D. G. Wilkinson, N. Holder, Nature 381, 319 (1996).
8. M. Nakamoto et al., Cell 86, 755 (1996).
9. M. Henkemeyer et al., Oncogene 9, 1001 (1994).
10. E. B. Pasquale, Cell Regul. 2, 523 (1991).
11. N. Becker et al., Mech. Dev. 47, 3 (1994).
12. M. Henkemeyer et al., Cell 86, 35 (1996).
13. D. Orioli, M. Henkemeyer, G. Lemke, R. Klein, T. Pawson, EMBO J. 15, 6035 (1996).
14. J. A. Holash and E. B. Pasquale, Dev. Biol. 172, 683 (1995).
15. M. P. Beckmann et al., EMBO J. 13, 3757 (1994).
16. B. D. Bennett et al., Proc. Natl. Acad. Sci. U.S.A. 92, 1866 (1995).
17. A. D. Bergemann, H.-J. Cheng, R. Brambilla, R. Klein, J. G. Flanagan, Mol. Cell. Biol. 15, 4921 (1995).
18. N. A. Nicola et al., Growth Factors 13, 141 (1996).
19. N. W. Gale et al., Oncogene 13, 1343 (1996).
20. Z. Songyang and L. C. Cantley, Trends Biochem. Sci. 20, 470 (1995).
21. N. Stahl et al., Science 267, 1349 (1995).
22. P. Bork and B. Margolis, Cell 80, 693 (1995).
23. T. Pawson, Nature 373, 573 (1995).
24. 2-HYEKVSGDYGHPVY-COOH (34). Polyclonal anti-Lerk2B was raised against a GST-Lerk2 cytoplasmic domain fusion protein (GST-Lerk2 cyto.) expressed in bacteria and purified by glutathione Sepharose (Pharmacia) affinity chromatography. Additional polyclonal antisera included anti-HAp against the hemagglutinin tag (HA. 11, Babco), anti-PDGF receptor (anti-PDGFR), and anti-cst1 against Src family kinases (from S. Courtneidge and G. Alonso). Mouse monoclonal antibodies included anti-HAm against the hemagglutinin tag (12CA5, Boehringer); anti-PY against phosphotyrosine (4G10, UBI); and 2-17, specific for Src (from S. Courtneidge and P. Lock).
25. Cek5-Fc and Lerk2-Fc fusion proteins (from Y. Whang-Zhu) were expressed and affinity-purified by Affigel protein A columns as described [H. Shao et al., J. Biol. Chem. 269, 26606 (1994)].
26. K. Brückner, E. B. Pasquale, R. Klein, data not shown.
27. Immunoprecipitates were subjected to kinase assays as described [R. M. Kypta et al., Cell 62, 481 (1990)]. Purified GST fusion proteins or acid-denatured enolase were added as exogenous substrates. The SH3 domain of the Fyn kinase was expressed as GST fusion protein (from P. Lock).
28. E. B. Pasquale, R. J. Connor, D. Rocholl, H. Schnürch, W. Risau, Dev. Biol. 163, 491 (1994).
29. S. Holland et al., Nature 383, 722 (1996).
30. A. Smits et al., Proc. Natl. Acad. Sci. U.S.A. 88, 8159 (1991).
31. R. F. Paulson, S. Vesely, K. A. Siminovitch, A. Bernstein, Nature Genet. 13, 309 (1996).
32. A. Goga et al., Oncogene 11, 791 (1995).
33. F. B. Gertler, R. L. Bennett, M. J. Clark, F. M. Hoffmann, Cell 58, 103 (1989).
34. Single-letter abbreviations for the amino acid residues are as follows: D, Asp; E, Glu; G, Gly; H, His; K, Lys; P, Pro; S, Ser; V, Val; and Y, Tyr.
35. Phe527 {pSGTSrc527; 50 ng [ T. Erpel et al., EMBO J. 14, 963 (1995)]}.
36. Phe527 {pSGTSrc527; 50 ng [ T. Erpel et al., EMBO J. 14, 963 (1995)]}.
37. Phe527 {pSGTSrc527; 50 ng [ T. Erpel et al., EMBO J. 14, 963 (1995)]}.
38. We thank S. Courtneidge, P. Lock, G. Alonso, C.-H. Heldin, and Y. Wang-Zhu for reagents; R. Brambilla for cell lines; F. Peverali, A. Nebreda, G. Lemke, and T. Graf for helpful discussions; and G. Superti-Furga, P. Orban, and R. Adams for critically reading the manuscript. K.B. is supported by an EMBL predoctoral fellowship. Supported in part by grants from the Deutsche Forschungsgemeinschaft (KI 948/1-1) and NIH (EY10576).