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BY-NC-ND 3.0 license Open Access Published by De Gruyter February 25, 2012

Enrichment strategies for phosphoproteomics: state-of-the-art

Barbora Salovska, Ales Tichy, Martina Rezacova, Jirina Vavrova and Eva Novotna

Abstract

Protein phosphorylation is a key regulator in many biological processes, such as homeostasis, cellular signaling and communication, transcriptional and translational regulation, and apoptosis. The defects in this tightly controlled reversible post-translational modification have been described to contribute to genesis and progression of various diseases, emphasizing the importance of a systematic research of this phenomenon. Although considerable effort has been devoted to improving the analysis of phosphorylation by mass spectrometry, which is currently the method of choice to study protein phosphorylation, the detection and identification of phosphorylation sites remains challenging because of the low abundance and low ionization efficacy of phosphoproteins in comparison with nonphosphorylated proteins. To overcome this obstacle, different enrichment strategies for phosphorylated peptides/proteins have been established and optimized for subsequent mass spectrometry analysis. In this review, we will give an overview of the methods currently available for the enrichment of phosphorylated proteins and peptides including immunoprecipitation, chemical derivatization and affinity enrichment techniques.


Corresponding author

Received: 2011-10-7
Accepted: 2012-1-13
Published Online: 2012-02-25
Published in Print: 2012-03-01

©2012 by Walter de Gruyter Berlin Boston

This article is distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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