The p110 gamma PI-3 kinase is required for EphA8-stimulated cell migration
- Gu, C; Park, S
- Issue Date
- ELSEVIER SCIENCE BV
- Eph; ephrin; p110 gamma PI-3 kinase
- FEBS LETTERS, v.540, no.1-3, pp.65 - 70
- Journal Title
- FEBS LETTERS
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- End Page
- This study provides evidence that treatment with preclustered ephrin A5-Fc results in a substantial increase in the stability of the p110gamma PI-3 kinase associated with EphA8, thereby enhancing PI-3 kinase activity and cell migration on a fibronectin substrate. In contrast, co-expression of a lipid kinase-inactive p110gamma mutant together with EphA8 inhibits ligand-stimulated PI-3 kinase activity and cell migration on a fibronectin substrate, suggesting that the mutant has a dominant negative effect against the endogenous p110gamma PI-3 kinase. Significantly, the tyrosine kinase activity of EphA8 is not important for either of these processes. Taken together, our results demonstrate that the stimulation of cell migration on a fibronectin substrate by the EphA8 receptor depends on the p110gamma PI-3 kinase but is independent of a tyrosine kinase activity. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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