Role of focal adhesion kinase in MAP kinase activation by insulin-like growth factor-I or insulin

• Published in: FEBS letters 1999-07, Vol.454 (3), p.252-256
• Main Authors: Arbet-Engels, Christophe, Janknecht, Ralf, Eckhart, Walter
• Format: Article
• Language: English
• Subjects: Animals; Calcium-Calmodulin-Dependent Protein Kinases - metabolism; Cell Adhesion Molecules - metabolism; Cell Line; Enzyme Activation - drug effects; FAK, focal adhesion kinase; Focal adhesion kinase; Focal Adhesion Kinase 1; Focal Adhesion Protein-Tyrosine Kinases; GST, glutathione S-transferase; Humans; Hypoglycemic Agents - metabolism; Hypoglycemic Agents - pharmacology; IGF-I, insulin-like growth factor-I; IGF-IR, IGF-I receptor; Insulin; Insulin - metabolism; Insulin - pharmacology; Insulin-like growth factor; Insulin-Like Growth Factor I - metabolism; Insulin-Like Growth Factor I - pharmacology; IR, insulin receptor; MAP kinase, mitogen-activated protein kinase; Mice; Mitogen-activated protein kinase; Protein-Tyrosine Kinases - metabolism; Src
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(99)00815-7

Integrin-induced focal adhesion kinase (FAK) phosphorylation as well as insulin-like growth factor-I (IGF-I) and insulin activate MAP kinase. Since IGF-I or insulin have been suggested to affect FAK phosphorylation, we analyzed the role of FAK in IGF-I- or insulin-induced MAP kinase activation. Although MAP kinase was stimulated by IGF-I or insulin, FAK tyrosine phosphorylation remained unchanged in fibroblasts expressing normal or transiently elevated levels of IGF-I and insulin receptors. Further analysis in FAK deficient fibroblasts suggested that FAK impedes MAP kinase activation by IGF-I or insulin.