Issue 10, 2009

Receptor tyrosine kinase signaling: a view from quantitative proteomics

Abstract

Growth factor receptor signaling via receptor tyrosine kinases (RTKs) is one of the basic cellular communication principals found in all metazoans. Extracellular signals are transferred viamembrane spanning receptors into the cytoplasm, reversible tyrosinephosphorylation being the hallmark of all RTKs. In recent years proteomic approaches have yielded detailed descriptions of cellular signaling events. Quantitative proteomics is able to characterize the exact position and strength of post-translational modifications (PTMs) providing essential information for understanding the molecular basis of signal transduction. Numerous new post-translational modification sites have been identified by quantitative mass spectrometry-based proteomics. In addition, plentiful new players in signal transduction have been identified underlining the complexity and the modular architecture of most signaling networks. In this review, we outline the principles of signal transductionvia RTKs and highlight some of the new insights obtained from proteomic approaches such as protein microarrays and quantitative mass spectrometry.

Graphical abstract: Receptor tyrosine kinase signaling: a view from quantitative proteomics

Article information

Article type
Review Article
Submitted
13 May 2009
Accepted
30 Jun 2009
First published
06 Aug 2009

Mol. BioSyst., 2009,5, 1112-1121

Receptor tyrosine kinase signaling: a view from quantitative proteomics

J. Dengjel, I. Kratchmarova and B. Blagoev, Mol. BioSyst., 2009, 5, 1112 DOI: 10.1039/B909534A

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