Activation of EphA receptor tyrosine kinase inhibits the Ras/MAPK pathway

Interactions between Eph receptor tyrosine kinases (RTKs) and membrane-anchored ephrin ligands critically regulate axon pathfinding and development of the cardiovascular system, as well as migration of neural cells. Similar to other RTKs, ligand-activated Eph kinases recruit multiple signalling and...

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Veröffentlicht in:	Nature cell biology 2001-05, Vol.3 (5), p.527-530
Hauptverfasser:	Miao, Hui, Wei, Bih-Rong, Peehl, Donna M., Li, Qing, Alexandrou, Terry, Schelling, Jeffrey R., Rhim, Johng S., Sedor, John R., Burnett, Elisabeth, Wang, Bingcheng
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Apoptosis Biomedical and Life Sciences brief-communication Cancer Research Cardiovascular system Cell Biology Cell Division Cell growth Cell Line Cell receptors Developmental Biology Endothelial Growth Factors - metabolism Enzyme Activation Enzyme Inhibitors - pharmacology Ephrin-A1 Epidermal Growth Factor - metabolism Fibroblasts Fibroblasts - metabolism Growth factors Humans Immunoblotting Keratinocytes - metabolism Kinases Life Sciences Ligands Lymphokines - metabolism Male MAP Kinase Signaling System Mitogen-Activated Protein Kinase 1 - antagonists & inhibitors Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases - antagonists & inhibitors Phosphatase Physiological aspects Platelet-Derived Growth Factor - metabolism Precipitin Tests Prostatic Neoplasms - metabolism Protein kinases Proteins - metabolism ras Proteins - antagonists & inhibitors ras Proteins - metabolism Rats Receptor Protein-Tyrosine Kinases - metabolism Receptor, EphA1 Receptor, EphA2 Rodents Signal Transduction Stem Cells Time Factors Tumor Cells, Cultured Vascular Endothelial Growth Factor A Vascular Endothelial Growth Factors
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