Both these authors contributed equally.
Quantitative phosphoproteomics by mass spectrometry: Past, present, and future
Article first published online: 7 OCT 2008
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Special Issue: SIGNAL TRANSDUCTION PROTEOMICS
Volume 8, Issue 21, pages 4433–4443, No. 21 November 2008
How to Cite
Nita-Lazar, A., Saito-Benz, H. and White, F. M. (2008), Quantitative phosphoproteomics by mass spectrometry: Past, present, and future. Proteomics, 8: 4433–4443. doi: 10.1002/pmic.200800231
- Issue published online: 28 OCT 2008
- Article first published online: 7 OCT 2008
- Manuscript Received: 12 MAR 2008
- Electrospray ionization-tandem mass spectrometry;
- Protein phosphorylation;
- Signal transduction profiling;
Protein phosphorylation-mediated signaling networks regulate much of the cellular response to external stimuli, and dysregulation in these networks has been linked to multiple disease states. Significant advancements have been made over the past decade to enable the analysis and quantification of cellular protein phosphorylation events, but comprehensive analysis of the phosphoproteome is still lacking, as is the ability to monitor signaling at the network level while comprehending the biological implications of each phosphorylation site. In this review we highlight many of the technological advances over the past decade and describe some of the latest applications of these tools to uncover signaling networks in a variety of biological settings. We finish with a concise discussion of the future of the field, including additional advances that are required to link protein phosphorylation analysis with biological insight.