Characterization of the EphA1 Receptor Tyrosine Kinase: Expression in Epithelial Tissues

References

• Boyd A. W, Ward L. D, Wicks I. P, Simpson R. J, Salvaris E. E., Wilks A., Welch K., Loudovaris M., Rockman S., Busmanis I. Isolation and characterization of a novel receptor-type protein tyrosine kinase (hek) from a human pre-B cell line. J. of Biol. Chem. 1992; 267: 3262–3267
   PubMedGoogle Scholar
• Bruce V., Olivieri G., Eickelberg O., Miescher G. C. Functional activation of EphAS receptor does not promote cell proliferation in the aberrant EphA5 expressing human glioblastoma U-118 MG cell line. Brain Res. 1999; 821: 169–176
   PubMedGoogle Scholar
• Connor R. J, Pasquale E. B. Genomic organization and alternatively processed forms of Cek5, a receptor protein-tyrosine kinase of the Eph subfamily. Oncogene 1995; 11: 2429–2438
   PubMedGoogle Scholar
• Davis S., Gale N. W, Aldrich T. H, Maisonpierre P. C, Lhotak V., Pawson T., Goldfarb M., Yancopoulos G. D. Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity. Science 1994; 266: 816–819
   PubMed Web of Science ®Google Scholar
• Doetschman T. C, Eistetter H., Katz M., Schmidt W., Kemler R. The in vitro development of blastocyst-derived embryonic stem cell lines: formation of visceral yolk sac, blood islands and myocardium. J. Embryol. Exp. Morphol. 1985; 87: 27–45
   PubMedGoogle Scholar
• Dottori M., Hartley L., Galea M., Paxinos G., Polizzotto M., Kilpatrick T., Bartlett P. P, Murphy M., Kontgen F., Boyd A. W. EphA4 (Sekl) receptor tyrosine kinase is required for the development of the corticospinal tract. Proc. Natl. Acad. Sci. U.S.A. 1998; 95: 13248–13253
   PubMedGoogle Scholar
• Easty D. J, Guthrie B. A, Maung K., Farr C. J, Lind-Berg R. A., Toso R. J, Herlyn M., Bennett D. C. Protein B61 as a new growth factor: expression of B61 and up-regulation of its receptor epithelial cell kinase during melanoma progression. Cancer Res. 1995; 55: 2528–2532
   PubMedGoogle Scholar
• Easty D. J, Hill S. P, Hsu M. Y, Fallowfield M. E, Florenes V. A, Herlyn M., Bennett D. C. Up-regulation of ephrin-Al during melanoma progression. Int. J. Cancer 1999; 84: 494–501
   PubMed Web of Science ®Google Scholar
• Elliott R. W., Moore K. J. Mouse chromosome 6. Mamm. Genome 1994; 79–103
   Google Scholar
• Ellis C., Kasmi F., Ganju P., Walls E., Panayotou G., Reith A. D. A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn. Oncogene 1996; 12: 1727–1736
   PubMedGoogle Scholar
• Evans E. P. Genetic Variants and Strains of the Laboratory Mouse, M. P. Lyon, A. Searle. Oxford University Press, Oxford 1989; 576–577
   Google Scholar
• Frisen J., Holmberg J., Barbacid M. Ephrins and their Eph receptors: multitalented directors of embryonic development. EMBO J. 1999; 18: 5159–5165
   PubMed Web of Science ®Google Scholar
• Gale N. W, Holland S. J, Valenzuela D. M, Flenniken A., Pan L., Ryan I. E, Hirai H., Wilkinson D. G, Pawson T., Davis S., Yancopoulos G. D. EPH Receptors and Ligands Comprise Two Major Specificity Subclasses and are Reciprocally Compartmentalized during Embryogenesis. Neuron 1996; 17: 9–19
   PubMed Web of Science ®Google Scholar
• Gerety S. S, Wang H. U, Chen Z. F, Anderson D. J. Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development [In Process Citation]. Mol. Cell 1999; 4: 403–414
   PubMed Web of Science ®Google Scholar
• Hanks S. K, Quinn A. M, Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988; 241: 42–52
   PubMed Web of Science ®Google Scholar
• Himanen J. P, Henkemeyer M., Nikolov D. B. Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2. Nature 1998; 396: 486–491
   PubMedGoogle Scholar
• Hirai H., Maru Y., Hagiwara K., Nishida J., Takaku F. A novel putative tyrosine kinase receptor encoded by the eph gene. Science 1987; 238: 1717–1720
   PubMed Web of Science ®Google Scholar
• Hock B., Bohme B., Karn T., Feller S., Rubsamen-Waigmann H., Strebhardt K. Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions. Oncogene 1998; 17: 255–260
   PubMedGoogle Scholar
• Holder N., Klein R. Eph receptors and ephrins: effectors of morphogenesis. Development 1999; 126: 2033–2044
   PubMed Web of Science ®Google Scholar
• Holland S. J, Gale N. W, Gish G. D, Roth R. A, Song Z. Yang, Cantley L. C, Henkemeyer M., Yancopoulos G. D, Pawson T. Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells. EMBO J. 1997; 16: 3877–3888
   PubMed Web of Science ®Google Scholar
• Kiyokawa E., Takai S., Tanaka M., Iwase T., Suzuki M., Xiang Y. Y, Naito Y., Yamada K., Sugimura H., Kino I. Overexpression of ERK, an EPH family receptor protein tyrosine kinase, in various human tumors. Cancer Res. 1994; 54: 3645–3650
   PubMed Web of Science ®Google Scholar
• Kozak M. The scanning model for translation: an update. Mol. Cell Biol. 1989; 9: 229–241
   Google Scholar
• Labrador J. P, Brambilla R., Klein R. The N-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling. EMBO J. 1997; 16: 3889–3897
   PubMedGoogle Scholar
• Lackmann M., Bucci T., Mann R. J, Kravets L. A, Viney E., Smith F., Moritz R. L, Carter W., Simpson R. J, Nicola N. A, Mackwell K., Nice E. C, Wilks A. F, Boyd A. W. Purification of a ligand for the EPH-like receptor HEK using a biosensor-based affinity detection approach. Proc. Natl. Acad. Sci. U.S.A. 1996; 93: 2523–2527
   PubMedGoogle Scholar
• Lackmann M., Mann R. J, Kravets L., Smith F. M, Bucci T. A, Maxwell K. F, Howlett G. J, Olsson J. E, Vanden Bos T., Cerretti D. P, Boyd A. W. Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor. J. Biol. Chem. 1997; 272: 16521–16530
   PubMedGoogle Scholar
• Lackmann M., Oates A. C, Dottori M., Smith P. M, Do C., Power M., Kravets L., Boyd A. W. Distinct sub-domains of the EphA3 receptor mediate ligand binding and receptor dimerization. J. Biol. Chem. 1998; 273: 20228–20237
   PubMedGoogle Scholar
• Lemke G. A Coherent Nomenclature for Eph Receptors and Their Ligands. Mol. Cell Neurosci. 1997; 9: 331–332
   PubMedGoogle Scholar
• Lemke G. Eph receptors and ligands in axon pathway choice, target recognition, and synaptogenesis. Prog. Brain Res. 1998; 117: 171–176
   PubMedGoogle Scholar
• Lickliter J. D, Smith F. M, Olsson J. E, Mackwell K. L, Boyd A. W. Embryonic stem cells express multiple Eph-subfamily receptor tyrosine kinases. Proc. Natl. Acad. Sci. U.S.A. 1996; 93: 145–150
   PubMed Web of Science ®Google Scholar
• Lindberg R. A, Hunter T. cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases. Mol. Cell Biol. 1990; 10: 6316–6324
   PubMed Web of Science ®Google Scholar
• Maru Y., Hirai H., Takaku F. Overexpression confers an oncogenic potential upon the eph gene. Oncogene 1990; 5: 445–447
   PubMedGoogle Scholar
• Maru Y., Hirai H., Yoshida M. C, Takaku F. Evolution, expression, and chromosomal location of a novel receptor tyrosine kinase gene, eph. Mol. Cell. Biol. 1988; 8: 3770–3776
   PubMedGoogle Scholar
• Miao H., Burnett E., Kinch M., Simon E., Wang B. Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation. Nat. Cell Biol. 2000; 2: 62–69
   PubMed Web of Science ®Google Scholar
• Mizushima S., Nagata S. pEF-BOS, a powerful mammalian expression vector. Nucleic Acids Res. 1990; 18: 5322
   PubMed Web of Science ®Google Scholar
• Nesbitt M. N., Francke U. A system of nomenclature for band patterns of mouse chromosomes. Chromosoma 1973; 41(2)145–158
   PubMedGoogle Scholar
• Oates A. C, Lackmann M., Power M. A, Brennan C., Smith F. M, Do C., Evans B., Holder N., Boyd A. W. An early developmental role for eph-ephrin interaction during vertebrate gastrulation. Mech. Dev. 1999; 83: 77–94
   PubMedGoogle Scholar
• O'Leary D. D., Wilkinson D. G. Eph receptors and ephrins in neural development. Curr. Opin. Neurobiol. 1999; 9: 65–73
   PubMedGoogle Scholar
• Owshalimpur D., Kelley M. J. Genomic structure of the EPHA1 receptor tyrosine kinase gene. Mol. Cell Probes 1999; 13: 169–173
   PubMedGoogle Scholar
• Patthy L. Intron-dependent evolution: preferred types of exons and introns. FEBS Lett. 1987; 214: 1–7
   PubMed Web of Science ®Google Scholar
• Robinson D., He F., Pretlow T., Kung H. J. A tyrosine kinase profile of prostate carcinoma. Proc. Natl. Acad. Sci. U.S.A. 1996; 93: 5958–5962
   PubMedGoogle Scholar
• Rosen B., Beddington R. S. Whole-mount in situ hybridization in the mouse embryo: gene expression in three dimensions. Trends Genet 1993; 9: 162–167
   PubMedGoogle Scholar
• Sambrook J., Fritsch E. F., Manniatis T. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY 1989
   Google Scholar
• Schultz J., Ponting C. P, Hofmann K., Bork P. SAM as a protein interaction domain involved in developmental regulation. Protein Science 1997; 6: 249–253
   PubMed Web of Science ®Google Scholar
• Shen M. M, Leder P. Leukemia inhibitory factor is expressed by the preimplantation uterus and selectively blocks primitive ectoderm formation in vitro. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 8240–8244
   PubMed Web of Science ®Google Scholar
• Stapleton D., Balan I., Pawson T., Sicheri F. The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization. Nat. Struct. Biol. 1999; 6: 44–49
   PubMedGoogle Scholar
• Stein E., Cerretti D. P, Daniel T. O. Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells. J. of Biol. Chem. 1996; 271: 23588–23593
   PubMedGoogle Scholar
• Stein E., Lane A. A, Cerretti D. P, Schoecklmann H. O, Schroff A. D, Van Etten R. L, Daniel T. O. Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses. Genes Dev. 1998; 12: 667–678
   PubMedGoogle Scholar
• Steube K. G, Meyer C., Habig S., Uphoff C. C, Drexler H. G. Expression of receptor tyrosine kinase HTK (hepatoma transmembrane kinase) and HTK ligand by human leukemia-lymphoma cell lines. Leuk. Lymphoma 1999; 33: 371–376
   PubMed Web of Science ®Google Scholar
• Sulman E. P, Tang X. X, Allen C., Biegel J. A, Pleasure D. E, Brodeur G. M, Ikegaki N. ECK, a human EPH-related gene, maps to Ip36.1, a common region of alteration in human cancers. Genomics 1997; 40: 371–374
   PubMed Web of Science ®Google Scholar
• Tang X. X, Brodeur G. M, Campling B. G, Ikegaki N. Coexpression of transcripts encoding EPHB receptor protein tyrosine kinases and their ephrin-B ligands in human small cell lung carcinoma. Clin. Cancer Res. 1999a; 5: 455–460
   PubMedGoogle Scholar
• Tang X. X, Evans A. E, Zhao H., Cnaan A., London W., Cohn S. L, Brodeur G. M, Ikegaki N. High-level expression of EPHB6, EFNB2, and EFNB3 is associated with low tumor stage and high TrkA expression in human neuroblastomas. Clin. Cancer Res. 1999b; 5: 1491–1496
   PubMedGoogle Scholar
• Torres R., Firestein B. L, Dong H., Staudinger J., Olson E. N, Huganir R. L, Bredt D. S, Gale N. W, Yancopoulos G. D. PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands [see comments]. Neuron 1998; 21: 1453–1463
   PubMed Web of Science ®Google Scholar
• Tsui L. C, Farrall M., Donis-Keller H. Report of the committee on the genetic constitution of chromosomes 7 and 8. Cytogenet. Cell Genet. 1989; 51: 166–201
   PubMedGoogle Scholar
• van Ewijk W. T-cell differentiation is influenced by thymic microenvironments. Annu. Rev. Immunol. 1991; 9: 591–615
   PubMed Web of Science ®Google Scholar
• Vogt T., Stolz W., Welsh J., Jung B., Kerbel R. S, Kobayashi H., Landthaler M., McClelland M. Overexpression of Lerk-5/Eplg5 messenger RNA: a novel marker for increased tumorigenicity and metastatic potential in human malignant melanomas. Clin. Cancer Res. 1998; 4: 791–797
   PubMedGoogle Scholar
• von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986; 14: 4683–4690
   PubMed Web of Science ®Google Scholar
• Wang H. U, Chen Z. F, Anderson D. J. Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4 [see comments]. Cell 1998; 93: 741–753
   PubMed Web of Science ®Google Scholar
• Webb G. C, Lee J. S, Campbell H. D, Young I. G. The genes for interleukins 3 and 5 map to the same locus on mouse chromosome 11. Cytogenet. Cell Genet. 1989; 50: 107–110
   PubMedGoogle Scholar
• Wicks I. P, Lapsys N. M, Baker E., Campbell L. J, Boyd A. W, Sutherland G. R. Localization of a human receptor tyrosine kinase (ETK1) to chromosome region 3p11.2. Genomics 1994; 19: 38–41
   PubMedGoogle Scholar
• Wicks I. P, Wilkinson D., Salvaris E., Boyd A. W. Molecular cloning of HEK, the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 1611–1615
   PubMedGoogle Scholar
• Wiles M. V. Embryonic stem cell differentiation in vitro. Methods Enzymol. 1993; 225: 900–918
   PubMedGoogle Scholar
• Wilkinson D. G. Eph receptors and ephrins: regulators of guidance and assembly [In Process Citation]. Int. Rev. Cytol. 2000; 196: 177–244
   PubMedGoogle Scholar
• Winning R. S, Scales J. B, Sargent T. D. Disruption of cell adhesion in Xenopus embryos by Pagliaccio, an Eph-class receptor tyrosine kinase. Dev. Biol. 1996; 179: 309–319
   PubMedGoogle Scholar
• Zetter B. R. Adhesion molecules in tumor metastasis [see comments]. Semin. Cancer Biol. 1993; 4: 219–229
   PubMed Web of Science ®Google Scholar
• Zisch A. H, Kalo M. S, Chong L. D, Pasquale E. B. Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region. Oncogene 1998; 16: 2657–2670
   PubMedGoogle Scholar
• Zou J. X, Wang B., Kalo M. S, Zisch A. H, Pasquale E. B, Ruoslahti E. An Eph receptor regulates integrin activity through R-Ras. Proc. Natl. Acad. Sci. U.S.A. 1999; 96: 13813–13818
   PubMed Web of Science ®Google Scholar