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Trends Plant Sci. 2009 Feb;14(2):71-6. doi: 10.1016/j.tplants.2008.11.003. Epub 2009 Jan 21.

Protein tyrosine phosphorylation in plants: More abundant than expected?

Author information

1
Department of Plant Molecular Biology, Max F. Perutz Laboratories, University of Vienna, Dr. Bohr-Gasse 9, 1030 Vienna, Austria.

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.

PMID:
19162527
DOI:
10.1016/j.tplants.2008.11.003
[Indexed for MEDLINE]

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