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Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions

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• Published: 17 July 1998

Oncogene volume 17, pages 255–260 (1998)Cite this article

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HEK2 belongs to the family of EPH-related receptor tyrosine kinases (RTK) which are involved in axonal pathfinding and the formation of the embryonic body plan. The knowledge about intracellular pathways of signal transduction mediated by EPH-related receptors is still limited. Many of the known key players of cellular signalling contain Src homology 2 (SH2) domains, which recognize phosphotyrosine motifs in RTKs. Thus, we examined the interactions of various SH2-containing molecules like PLC-γ1, rasGAP, p85 subunit of PI3-kinase, Src, Fyn, Crk, Nck, Grb2 and Shc with HEK2 using in vitro binding assays, immunoprecipitations and yeast Two-Hybrid assays. We found that rasGAP, Crk and Fyn bind in a SH2-dependent manner to autophosphorylated HEK2. rasGAP, which contains two SH2- and one SH3-domain, was shown to associate with its N-terminal SH2-domain to HEK2. Furthermore, we demonstrated that a single amino acid substitution (Y614F) clearly reduces the phosphotyrosine content of HEK2 and abrogates its ability to bind rasGAP, Crk and Fyn indicating that this residue functions as major phosphorylation and multi-docking site. The conservation of this predicted binding site among various EPH-related RTKs provides evidence that Fyn, Crk and rasGAP are key players in signal transduction of at least a subset of these receptors.

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1. Björn Hock and Beatrix Böhme: Björn Hock and Beatrix Böhme made equal contributions to this work

1. Chemotherapeutisches Forschungsinstitut, Georg-Speyer-Haus, Paul-Ehrlich-Str. 42-44, Frankfurt, 60596, Germany

   Björn Hock, Beatrix Böhme, Thomas Karn & Klaus Strebhardt

2. Labor für Molekulare Onkologie, Medizinisches Institut für Strahlenkunde & Zellforschung (MSZ), Versbacherstr. 5, Würzburg, 97078, Germany

   Stephan Feller

3. Bayer AG, Institut für Virologie, Wuppertal, 42096, Germany

   Helga Rübsamen-Waigmann

1. Björn Hock
2. Beatrix Böhme
3. Thomas Karn
4. Stephan Feller
5. Helga Rübsamen-Waigmann
6. Klaus Strebhardt

Hock, B., Böhme, B., Karn, T. et al. Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions. Oncogene 17, 255–260 (1998). https://doi.org/10.1038/sj.onc.1201907

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• Received: 03 October 1997

• Revised: 13 February 1998

• Accepted: 13 February 1998

• Published: 17 July 1998

• Issue Date: 16 July 1998

• DOI: https://doi.org/10.1038/sj.onc.1201907

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