Development of a 5-plex SILAC method tuned for the quantitation of tyrosine phosphorylation dynamics.

ABSTRACT: The propagation of phosphorylation downstream of receptor tyrosine kinases is a key dynamic cellular event involved in signal transduction, which is often deregulated in disease states such as cancer. Probing phosphorylation dynamics is therefore crucial for understanding receptor tyrosine kinases' function and finding ways to inhibit their effects. MS methods combined with metabolic labeling such as stable isotope labeling with amino acids in cell culture (SILAC) have already proven successful in deciphering temporal phosphotyrosine perturbations. However, they are limited in terms of multiplexing, and they also are time consuming, because several experiments need to be performed separately. Here, we introduce an innovative approach based on 5-plex SILAC that allows monitoring of phosphot

SUBMITTER: Tzouros M 

PROVIDER: S-EPMC3820944 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature