Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.273.17.10682
Title: Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2: FAK is not required for stat- mediated transcription
Authors: Zhu, T. 
Goh, E.L.K. 
Lobie, P.E. 
Issue Date: 24-Apr-1998
Citation: Zhu, T., Goh, E.L.K., Lobie, P.E. (1998-04-24). Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2: FAK is not required for stat- mediated transcription. Journal of Biological Chemistry 273 (17) : 10682-10689. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.273.17.10682
Abstract: 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.
Source Title: Journal of Biological Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/115750
ISSN: 00219258
DOI: 10.1074/jbc.273.17.10682
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