Abstract
Tyrosine-specific phosphorylation of proteins is a key to the control of diverse pathways leading to cell growth and differentiation1. The protein-tyrosine kinases described to date are either transmembrane proteins having an extracellular ligand binding domain2–7 or cytoplasmic proteins related to the v-src oncogene8–10. Most of these proteins are expressed in a wide variety of cells and tissues; few are tissue-specific1. Previous studies have suggested that lymphokines could mediate haematopoietic cell survival through their action on glucose transport11,12, regulated in some cells through the protein-tyrosine kinase activity of the insulin receptor13. We have investigated the possibility that insulin receptor-like genes are expressed specifically in haematopoietic cells. Using the insulin receptor-related avian sarcoma oncogene v-ros as a probe14, we have isolated and characterized the complementary DNA of a novel gene, ltk (leukocyte tyrosine kinase). The ltk gene is expressed mainly in leukocytes, is related to several tyrosine kinase receptor genes of the insulin receptor family and has unique structural properties: it apparently encodes a transmembrane protein devoid of an extracellular domain. Two candidate ltk proteins have been identified with antibodies in the mouse thymus, and have properties indicating that they are integral membrane proteins. These features suggest that ltk could be a signal transduction subunit for one or several of the haematopoietic receptors.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Hunter, T. Cell 50, 823–829 (1987).
Ebina, Y. et al. Cell 40, 747–758 (1985).
Ulrich, A. et al. Nature 313, 756–761 (1985).
Ulrich, A. et al. Nature 309, 418–425 (1984).
Yarden, Y. et al. Nature 323, 226–232 (1986).
Ulrich, A. et al. EMBO J. 5, 2508–2512 (1986).
Sherr, C. J. et al. Cell 41, 665–676 (1985).
Snyder, M. A., Bishop, J. M., Colby, W. W. & Levinson, A. D. Cell 32, 891–901 (1983).
Cross, F. R. & Hanafuza, H. Cell 34, 597–607 (1983).
Ben-Neriah, Y., Bernards, A., Paskind, M., Daley, G. Q. & Baltimore, D. Cell 44, 577–586 (1986).
Whetton, A. D., Bazill, G. W. & Dexter, M. T. EMBO J. 3, 409–413 (1984).
Dexter, M. T. et al. in Oncogenes and Growth Control (eds Kahn, P. & Graf, T.) 163–169 (Springer, Heidelberg, 1986).
Goldfine, I. D. Endocrine Rev. 8, 235–255 (1987).
Neckameyer, W. S. & Wang, L. H. J. Virol. 53, 879–884 (1985).
Hopp, T. P. & Woods, K. R. Proc. natn. Acad. Sci. U.S.A. 78, 3821–3824 (1981).
Matsushime, H., Wang, L. H. & Shibuya, M. Molec. cell. Biol. 6, 3000–3004 (1986).
Hafen, E., Basler, K., Edstroem, J. & Rubin, G. M. Science 236, 55–63 (1987).
Martin-Zanca, D., Hughes, S. H. & Barbacid, M. Nature 319, 743–748 (1986).
Yu, K. T., Peters, M. A. & Czech, M. D. J. biol. Chem. 261, 11341–11349 (1986).
Rosen, O. M., Herrara, R., Olowe, Y., Pelruzelli, L. M. & Cobb, M. H. Proc. natn. Acad. Sci. U.S.A. 80, 3237–3240 (1983).
Sibley, D. R., Benovic, J. L., Caron, M. G. & Lefkowitz, R. J. Cell 48, 913–922 (1987).
Azar, Y. et al. Cell. Immun. 65, 194–200 (1981).
Schejter, E. D. et al. Cell 46, 1091–1101 (1986).
Bordier, C. J. biol. Chem. 256, 1604–1607 (1981).
Gething, M. J., McCammon, K. & Sambrook, J. Cell 46, 939–950 (1986).
Smith, K. A. Immunol. Today 8, 11–13 (1987).
Nicola, N. A. Immunol. Today 8, 135–140 (1987).
Paul, W. E. & Ohara, J. A. Rev. Immun. 5, 429–459 (1987).
Sanger, F., Nicklen, S. & Coulson, A. R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).
Maxam, A. M. & Gilbert, W. Proc. natn. Acad. Sci. U.S.A. 74, 560–564 (1977).
Mizusawa, S., Nishimura, S. & Seela, F. Nucleic Acids Res. 14, 1319–1324 (1986).
Tabor, S. & Richardson, C. C. Proc. natn. Acad. Sci. U.S.A. 84, 4767–4771 (1987).
Berk, A. J. & Sharp, P. A. Cell 12, 721–732 (1977).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Ben-Neriah, Y., Bauskin, A. Leukocytes express a novel gene encoding a putative transmembrane protein-kinase devoid of an extracellular domain. Nature 333, 672–676 (1988). https://doi.org/10.1038/333672a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/333672a0
This article is cited by
-
Anaplastic lymphoma kinase overexpression enhances aggressive phenotypic characteristics of endometrial carcinoma
BMC Cancer (2023)
-
Structural basis of cytokine-mediated activation of ALK family receptors
Nature (2021)
-
Functional role of ALK-related signal cascades on modulation of epithelial-mesenchymal transition and apoptosis in uterine carcinosarcoma
Molecular Cancer (2017)
-
Heart-specific activation of LTK results in cardiac hypertrophy, cardiomyocyte degeneration and gene reprogramming in transgenic mice
Oncogene (1999)
-
Neu receptor dimerization
Nature (1989)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.