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Updated: Oct 28, 2025

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Phosphorylation Site Motifs in Plant Protein Kinases and Their Substrates
Lin Xi1, Zhaoxia Zhang2, Sandra Herold2
1Department of Plant Systems Biology, University of Hohenheim, Stuttgart, Germany. lin.xi.260@uni-hohenheim.de.
Abstract:
Protein phosphorylation is an important cellular regulatory mechanism affecting the activity, localization, conformation, and interaction of proteins. Protein phosphorylation is catalyzed by kinases, and thus kinases are the enzymes regulating cellular signaling cascades. In the model plant Arabidopsis, 940 genes encode for kinases. The substrate proteins of kinases are phosphorylated at defined sites, which consist of common patterns around the phosphorylation site, known as phosphorylation motifs. The discovery of kinase specificity with a preference of phosphorylation of certain motifs and application of such motifs in deducing signaling cascades helped to reveal underlying regulation mechanisms, and facilitated the prediction of kinase-target pairs. In this mini-review, we took advantage of retrieved data as examples to present the functions of kinase families along with their commonly found phosphorylation motifs from their substrates.
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