Journal
PROTEOMICS
Volume 16, Issue 14, Pages 1992-1997Publisher
WILEY
DOI: 10.1002/pmic.201600118
Keywords
Cell Biology; PHOSIDA; Phosphoproteomics; PI3K; Signaling
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The PI3K pathway is commonly activated in cancer. Only a few studies have attempted to explore the spectrum of phosphorylation signaling downstream of the PI3K cascade. Such insight, however, is imperative to understand the mechanisms responsible for oncogenic phenotypes. By applying MS-based phosphoproteomics, we mapped 2509 phosphorylation sites on 1096 proteins, and quantified their responses to activation or inhibition of PIK3CA using isogenic knock-in derivatives and a series of targeted inhibitors. We uncovered phosphorylation changes in a wide variety of proteins involved in cell growth and proliferation, many of which have not been previously associated with PI3K signaling. A significant update of the posttranslational modification database PHOSIDA () allows efficient use of the data. All MS data have been deposited in the ProteomeXchange with identifier PXD003899 ().
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