Oxidation of Akt2 kinase promotes cell migration and regulates G1-S transition in the cell cycle |
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| Authors: | Revati Wani N Sharmila Bharathi Jeffrey Field Allen W Tsang Cristina M Furdui |
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| Affiliation: | 1.Section on Molecular Medicine; Department of Internal Medicine; Winston-Salem, NC USA;;3.Biochemistry; Wake Forest School of Medicine; Winston-Salem, NC USA;2.Department of Pharmacology; University of Pennsylvania School of Medicine; Philadelphia, PA, USA |
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| Abstract: | Phosphorylation has long been recognized as the key mediator of protein signaling. New modes of signaling regulation are emerging with the development of specific chemical probes and application of high-throughput mass spectrometry technologies. Using biotin-tagged chemical probes for protein oxidation, mass spectrometry and functional assays, our group has recently reported isoform-specific oxidation of Akt2 in response to PDGF signaling. The studies included here investigate the functional consequence of oxidation on Akt2-mediated cell migration and cell cycle. Akt2-KO MEFs transduced with WT and Cys124Ser Akt2 were used as the model system for these studies. The implications of these findings on disease pathology are discussed.Key words: oxidation, ROS, cell migration, cell cycle, wound healing, Akt2, starvation |
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