期刊
FEBS LETTERS
卷 583, 期 12, 页码 1987-1993出版社
WILEY
DOI: 10.1016/j.febslet.2009.05.011
关键词
Stress; Oxidant; Signal transduction; ERK1/2; Akt; Imaging; Quantitative immunofluorescence
ERK and Akt kinases are key components that participate in numerous regulatory processes, including the response to stress. Using novel tools for quantitative immunofluorescence, we show that oxidant exposure controls the intracellular activation and localization of ERK1/2 and Akt. Oxidative stress alters the nuclear/cytoplasmic levels of the kinases, drastically changing phospho-ERK1/2 and phospho-Akt(Ser473) levels in the nucleus. Moreover, pharmacological inhibition of PI3 kinase modulates the intracellular distribution of phospho-ERK1/2, whereas MEK inhibition affects phosphoAkt(Thr308) and phospho-Akt( Ser473). Our studies identify a new signaling link in the nucleus of stressed cells, where changes in phospho-ERK1/2 levels correlate directly with changes in phosphoAkt( Ser473). (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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