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• W2038564346 abstract "We report here for the first time that the specific MAPK kinase (MEK) inhibitor, PD-98059, completely knocked out granulocyte-macrophage colony-stimulating factor (GM-CSF)-stimulated MAPK activity but also partially inactivated the ribosomal kinase p70S6K. Since a connection between the two major signaling pathways, Ras/MEK/MAPK and PI3-K/p70S6K was suspected, experiments were designed to prove a molecular crosstalk between those. First, p70S6K protein could be co-immunoprecipitated with anti-MAPK antibodies, MAPK protein was similarly present in anti-p70S6K immunoprecipitates, indicating close spatial proximity of both signaling molecules. Second, p70S6K enzymatic activity was found in anti-MAPK immunoprecipitates and MAPK in anti-p70S6K immunoprecipitates, being the latter activity higher in samples derived from GM-CSF-treated cells. Since an upstream activator of p70S6K, phosphatidylinositol (PI)3-kinase, has been associated to cell movement in phagocytic cells, we studied a possible participation of p70S6K in chemotaxis and whether MAPK had an input. Our data show that functional chemotaxis was inhibited by rapamycin, a specific p70S6K inhibitor, as well as by PD-98059. Thus, a connection between these two kinases extends from the molecular level to cell migration, a key functionality in non-proliferative, mature phagocytes such as neutrophils." @default.
• W2038564346 created "2016-06-24" @default.
• W2038564346 creator A5013404192 @default.
• W2038564346 creator A5081541163 @default.
• W2038564346 date "2002-04-01" @default.
• W2038564346 modified "2023-10-16" @default.
• W2038564346 title "Molecular crosstalk between p70S6k and MAPK cell signaling pathways" @default.
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• W2038564346 doi "https://doi.org/10.1016/s0006-291x(02)00238-3" @default.
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