Quantitative phosphoproteomic analysis of the PI3K‐regulated signaling network. Issue 14 (8th July 2016)

• Record Type: Journal Article
• Authors: Gnad, Florian; Wallin, Jeffrey; Edgar, Kyle; Doll, Sophia; Arnott, David; Robillard, Liliane; Kirkpatrick, Donald S.; Stokes, Matthew P.; Vijapurkar, Ulka; Hatzivassiliou, Georgia; Friedman, Lori S.; Belvin, Marcia
• Is Part Of: Proteomics. Volume 16:Issue 14(2016)
• Page Start: 1992
• Page End: 1997
• Publication Date: 2016-07-08
• Subjects: Cell Biology -- PHOSIDA -- Phosphoproteomics -- PI3K -- Signaling; Proteins -- Separation -- Periodicals; Bioinformatics -- Periodicals; Proteomics -- Periodicals; Genomes -- Periodicals; Molecular genetics -- Periodicals; 572.605
• DOI: 10.1002/pmic.201600118
• Languages: English
• ISSNs: 1615-9853

Abstract

Abstract : 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 (http://www.phosida.com ) allows efficient use of the data. All MS data have been deposited in the ProteomeXchange with identifier PXD003899 (http://proteomecentral.proteomexchange.org/dataset/PXD003899 ).