Characterisation of the Sek‐1 receptor tyrosine kinase
- 17 July 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 368 (2) , 353-357
- https://doi.org/10.1016/0014-5793(95)00652-p
Abstract
We present an initial characterisation of the mouse Sek‐1 protein, a member of the Eph subfamily of putative receptor tyrosine kinases, which has been proposed to play a role in the segmentation of both the hindbrain and the mesoderm. Antibodies raised against the protein have been used to confirm the early embryonic expression pattern previously established by mRNA in situ hybridisation. These antibodies, together with the expression of the Sek‐1 gene in a baculovirus system, were instrumental in demonstrating that the protein carries a tyrosine kinase activity and that it is presented at the cell surface with its N‐terminal (putative ligand‐binding) domain outside of the cell. Therefore, as expected from its amino acid sequence, Sek‐1 conforms to the general model of receptor‐type tyrosine kinases.Keywords
This publication has 27 references indexed in Scilit:
- Role of B61, the Ligand for the Eck Receptor Tyrosine Kinase, in TNF-α-Induced AngiogenesisScience, 1995
- Initial Tract Formation in the Brain of the Chick Embryo: Selective Expression of the BEN/SC1/DM‐GRASP Cell Adhesion MoleculeEuropean Journal of Neuroscience, 1995
- Receptor tyrosine kinase signalling: not so complex after all?Trends in Cell Biology, 1994
- Ligands for EPH-Related Receptor Tyrosine Kinases that Require Membrane Attachment or Clustering for ActivityScience, 1994
- B61 is a ligand for the ECK receptor protein-tyrosine kinaseNature, 1994
- An extended family of protein-tyrosine kinase genes differentially expressed in the vertebrate nervous systemNeuron, 1991
- Receptor tyrosine kinases: genetic evidence for their role in Drosophila and mouse developmentTrends in Genetics, 1990
- Signal transduction by receptors with tyrosine kinase activityPublished by Elsevier ,1990
- Direct activation of the serine/threonine kinase activity of raf-1 through tyrosine phosphorylation by the PDGF β-receptorCell, 1989
- Neural cell recognition molecule F11: Homology with fibronectin type III and immunoglobulin type C domainsNeuron, 1989