Isoform-specific regulation of Akt by PDGF-induced reactive oxygen species

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Abstract

Isoform-specific signaling of Akt, a major signaling hub and a prominent therapeutic target, remained poorly defined until recently. Subcellular distribution, tissue-specific expression, substrate specificity, and posttranslational modifications are believed to underlie isoform-specific signaling of Akt. The studies reported here show inhibition of Akt2 activity under physiologically relevant conditions of oxidation created by PDGF-induced reactive oxygen species. Combined MS and functional assays identified Cys124 located in the linker region between the N-terminal pleckstrin homology domain and the catalytic kinase domain as one of the unique regulatory redox sites in Akt2 with functional consequence on PDGF-stimulated glucose uptake. A model is proposed describing the consequence of increased endogenous oxidation induced by extracellular cues such as PDGF on Akt2 activity.

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APA

Wani, R., Qian, J., Yin, L., Bechtold, E., King, S. B., Poole, L. B., … Furdui, C. M. (2011). Isoform-specific regulation of Akt by PDGF-induced reactive oxygen species. Proceedings of the National Academy of Sciences of the United States of America, 108(26), 10550–10555. https://doi.org/10.1073/pnas.1011665108

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