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J. Cell Biol.,
Volume 145, Number 7, June 28, 1999 1461-1470
* Laboratory of Cell Adhesion and Signaling, Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer
Center, New York 10021; and The extracellular matrix exerts a stringent
control on the proliferation of normal cells, suggesting
the existence of a mitogenic signaling pathway activated by integrins, but not significantly by growth factor
receptors. Herein, we provide evidence that integrins cause a significant and protracted activation of Jun
NH2-terminal kinase (JNK), while several growth factors cause more modest or no activation of this enzyme.
Integrin-mediated stimulation of JNK required the association of focal adhesion kinase (FAK) with a Src kinase and p130CAS, the phosphorylation of p130CAS, and
subsequently, the recruitment of Crk. Ras and PI-3K
were not required. FAK-JNK signaling was necessary
for proper progression through the G1 phase of the cell
cycle. These findings establish a role for FAK in both
the activation of JNK and the control of the cell cycle,
and identify a physiological stimulus for JNK signaling
that is consistent with the role of Jun in both proliferation and transformation.
Laboratory of Molecular Oncology, The Rockefeller University, New York 10021
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