Epidermal growth factor stimulates serine/threonine phosphorylation of the focal adhesion protein paxillin in a MEK-dependent manner in normal rat kidney cells

Journal of Cellular Physiology
David R TerferaChristopher E Turner

Abstract

Epidermal growth factor (EGF)-stimulated proliferation of renal epithelial cells plays an important role in the recovery of kidney tubule epithelia following exposure to insult. Numerous studies have demonstrated that tyrosine phosphorylation of the focal adhesion protein paxillin mediates in part the effects of growth factors on cell growth, migration, and organization of the actin-based cytoskeleton. The experiments in this report were designed to determine the effect of EGF on paxillin phosphorylation in normal rat kidney (NRK) epithelial cells. Interestingly, treatment of NRK cells with EGF stimulated paxillin serine/threonine phosphorylation, which caused a reduction in the mobility of paxillin on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The EGF-stimulated mobility shift of paxillin was independent of an intact cytoskeleton, phosphatidylinositol 3-kinase (PI 3-kinase) activation, protein kinase C (PKC) activation, and cellular adhesion. However, inhibitors of the mitogen-activated protein kinase/extracellular signal-regulated kinase kinase abrogated the EGF-stimulated change in paxillin mobility. In addition, the EGF-stimulated change in paxillin serine/threonine phosphorylation was not accompa...Continue Reading

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Citations

May 3, 2003·Biochemical and Biophysical Research Communications·Motoyuki OgawaSadakazu Aiso
Jun 3, 2006·Cancer Research·Yasuaki TatsumiZigang Dong
Apr 8, 2006·The International Journal of Biochemistry & Cell Biology·Caryn L ElsegoodLe T Duong
Sep 27, 2005·Experimental Cell Research·Sara E HeteyChristopher E Turner
Jun 28, 2012·PLoS Computational Biology·Carlo ChanGermán Enciso
Sep 24, 2004·Physiological Reviews·Michael C Brown, Christopher E Turner

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