Premium
Quantitative phosphoproteomic analysis of the PI3K‐regulated signaling network
Author(s) -
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
Publication year - 2016
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201600118
Subject(s) - phosphoproteomics , phosphorylation , pi3k/akt/mtor pathway , signal transduction , biology , computational biology , proteomics , quantitative proteomics , microbiology and biotechnology , stable isotope labeling by amino acids in cell culture , protein phosphorylation , protein kinase a , biochemistry , gene
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).