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Role of focal adhesion kinase in MAP kinase activation by insulin‐likegrowth factor‐I or insulin
Author(s) -
C Arbet-Engels,
R Janknecht,
W Eckhart
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00815-7
Subject(s) - insulin receptor , focal adhesion , insulin , insulin receptor substrate , tyrosine kinase , microbiology and biotechnology , chemistry , tyrosine phosphorylation , map kinase kinase kinase , medicine , ptk2 , insulin like growth factor , cyclin dependent kinase 9 , endocrinology , mitogen activated protein kinase kinase , phosphorylation , cancer research , biology , signal transduction , protein kinase b , growth factor , protein kinase a , insulin resistance , biochemistry , receptor
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.