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Issue 10, 2009
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Receptor tyrosine kinase signaling: a view from quantitative proteomics

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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

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Publication details

The article was received on 13 May 2009, accepted on 30 Jun 2009 and first published on 06 Aug 2009


Article type: Review Article
DOI: 10.1039/B909534A
Citation: Mol. BioSyst., 2009,5, 1112-1121
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    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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