par Bousbata, Sabrina ;Bergoin, Alexis;Rossignol, Michel
Référence Plant physiology and biochemistry, 42, 12, page (929-936)
Publication Publié, 2004-12
Article révisé par les pairs
Résumé : Protein phosphorylation constitutes a major type of post-translational modification that mobilizes a high number of genes, especially in plants, is involved in many crucial cell functions and largely participates to the complexity of the proteomes. For several biological and technical reasons, the characterization of phosphorylation sites requires complex procedures. In this review, the different approaches presently available to select phosphoproteins and phosphopeptides are described. A special emphasis is then given to the numerous strategies that have emerged for the analysis of phosphorylation sites by various techniques of mass spectrometry. Finally, the few attempts proposed for the quantification of phosphorylation events are presented. In another part, the results of the efforts made in the plant area to analyze the phosphoproteome are compared to those in other biological systems. These overviews are put together to delineate, according to the objectives pursued, the different strategies possible and the corresponding challenges.