title: Proteomic analysis of phosphorylated proteins.
abstract: Reversible protein phosphorylation is of crucial importance in regulatory mechanisms and signaling pathways. Novel and efficient tools and strategies are being actively developed to allow, beyond the primary identification of phosphorylated proteins, the identification of phosphorylation sites and ultimately their quantification. These approaches are being used at various scales, from studies that have dedicated and functional goals to work with more exploratory and cataloguing objectives. The information thus generated now makes it possible to use bioinformatics to revisit previous knowledge about protein phosphorylation in plants and the pertinence of available prediction models. Although the analysis of phosphorylated proteins remains a challenging task, recent success and current developments are likely to mark the transition towards the introduction of phosphoproteomics as one of the main integration levels in post-genome plant biology.
authors.affiliation: INRA, Proteomics Laboratory, UR 1199, Place Viala 2, 34060 Montpellier Cedex 1, France. rossignol@ensam.inra.fr <rossignol@ensam.inra.fr>
authors.forename: Michel
authors.initials: M
authors.lastname: Rossignol
mesh_terms: D019295:Computational Biology; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D040901:Proteomics / Q000379:methods
chemical_list: D010940:Plant Proteins; D010770:Phosphotransferases