title: Protein tyrosine phosphorylation in plants: More abundant than expected?
abstract: Protein phosphorylation in eukaryotes predominantly occurs on serine (Ser) and threonine (Thr) residues, whereas phosphorylation on tyrosine (Tyr) residues is less abundant. Plants lack classic Tyr kinases, such as the epidermal growth factor receptor, that govern Tyr phosphorylation in animals. A long-standing debate questions whether plants have any Tyr-specific kinases and, although several protein kinases with both Ser/Thr and Tyr specificities exist, data supporting the existence of other such kinases are scarce. As we discuss here, mass-spectrometry-based analyses now indicate that Tyr phosphorylation is as extensive in plants as it is in animals. However, careful inspection of available data indicates that these promising mass spectrometry studies have to be interpreted with caution before current ideas on Tyr phosphorylation in plants are revised.
authors.affiliation: Department of Plant Molecular Biology, Max F. Perutz Laboratories, University of Vienna, Dr. Bohr-Gasse 9, 1030 Vienna, Austria.
authors.forename: Sergio
authors.initials: S
authors.lastname: de la Fuente van Bentem
authors.forename: Heribert
authors.initials: H
authors.lastname: Hirt
mesh_terms: D020134:Catalytic Domain; D013058:Mass Spectrometry; D010766:Phosphorylation / Q000502:physiology*; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism*
chemical_list: D010940:Plant Proteins; D014443:Tyrosine; D011494:Protein Kinases