Analysis of protein phosphorylation by mass spectrometry

Eur. J. Mass Spectrom. 10, 383–392 (2004)
DOI: 10.1255/ejms.601

Analysis of protein phosphorylation by mass spectrometry

Liliana B. Areces
European Institute of Oncology, Via Ripamonti 435, 20141 Milan, Italy
Vittoria Matafora and Angela Bachi^*
Dibit, San Raffaele Scientific Institute. Via Olgettina 58, 20132, Milan, Italy

ABSTRACT:

Phosphorylation is one of the most frequently occurring post-translational modifications in proteins. In eukaryotic cells, protein phosphorylation on serine, threonine and tyrosine residues plays a crucial role as a modulator of protein function. A comprehensive analysis of protein phosphorylation involves the identification of the phosphoproteins, the exact localization of the residues that are phosphorylated and the quantitation of phosphorylation. In this short review we will summarize and discuss the methodologies currently available for the analysis and full characterization of phosphoproteins with special attention at mass spectrometry-based techniques. In particular, we will discuss affinity-based purification of phosphopeptides coupled to MALDI-TOF analysis, their detection using mass mapping and precursor ion scan, identification of modified sites by MS/MS and quantitation analysis

Keywords: phosphoprotein, post-translational modifications, mass spectrometry, proteomics, quantitative analysis

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