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J Biol Chem, Vol. 273, Issue 17, 10682-10689, April 24, 1998
From the Institute of Molecular and Cell Biology and Defense
Medical Research Institute, National University of Singapore, 10 Kent
Ridge Crescent, Singapore 119260, Republic of Singapore
We have demonstrated that growth hormone (GH)
activates focal adhesion kinase (FAK), and this activation results in
the tyrosine phosphorylation of two FAK substrates, paxillin and
tensin. The activation of FAK is time-dependent (maximal
activation at 5-15 min) and dose-dependent (maximal
activation at 0.05 nM). FAK and paxillin are
constitutively associated in the unstimulated state, remain associated
during the stimulation phase, and recruit tyrosine-phosphorylated tensin to the complex after GH stimulation. Half of the
carboxyl-terminal region of the GH receptor is dispensable for FAK
activation, but FAK activation does require the proline-rich box 1 region of the GH receptor, indicative that FAK is downstream of JAK2.
FAK associates with JAK2 but not JAK1 after GH stimulation of cells.
Using FAK-replete and FAK-deficient cells, we also show that FAK is not
required for STAT-mediated transcriptional activation by GH. The use of FAK in the signal transduction pathway utilized by GH may be central to
many of the pleiotropic effects of GH, including cytoskeletal reorganization, cell migration, chemotaxis, mitogenesis, and/or prevention of apoptosis and gene transcription.
Growth Hormone Stimulates the Tyrosine Phosphorylation and
Association of p125 Focal Adhesion Kinase (FAK) with JAK2
FAK IS NOT REQUIRED FOR STAT-MEDIATED TRANSCRIPTION
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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