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Interplay between MEK and PI3 kinase signaling regulates the subcellular localization of protein kinases ERK1/2 and Akt upon oxidative stress
Author(s) -
Kodiha Mohamed,
Bański Piotr,
Stochaj Ursula
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.05.011
Subject(s) - protein kinase b , kinase , microbiology and biotechnology , mapk/erk pathway , subcellular localization , intracellular , cytoplasm , oxidative stress , chemistry , nucleus , signal transduction , biology , biochemistry
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 phospho‐Akt(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 phospho‐Akt(Ser473).