Receptor tyrosine kinase (RTK) mediated tyrosine phosphor-proteome from Drosophila S2 (ErbB1) cells reveals novel signaling networks.

ABSTRACT: Protein phosphorylation mediates many critical cellular responses and is essential for many biological functions during development. About one-third of cellular proteins are phosphorylated, representing the phosphor-proteome, and phosphorylation can alter a protein's function, activity, localization and stability. Tyrosine phosphorylation events mediated by aberrant activation of Receptor Tyrosine Kinase (RTK) pathways have been proven to be involved in the development of several diseases including cancer. To understand the systems biology of RTK activation, we have developed a phosphor-proteome focused on tyrosine phosphorylation events under insulin and EGF signaling pathways using the PhosphoScan technique coupled with high-throughput mass spectrometry analysis. Comparative proteomic an

SUBMITTER: Krishnamoorthy S 

PROVIDER: S-EPMC2488400 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature