Plant tyrosine kinases

Evolution of tyrosine kinases: Plant tyrosine kinases

Plants lack classical tyrosine kinases from the TK group, but do contain phosphotyrosine, dual-specificty kinases and some cryptic tyrosine kinases.

Evidence from Phosphoproteomics

Several phosphoproteomics scans in plants show substantial phosphotyrosine, at a level often comparable to that found in animals [1]. Much of this is found on substrates of known dual-specificity kinases: CDC2 (the substrate of Wee1), MAPK substrates of MAP2K kinases, and the autophosphorylation sites on DYRK family kinases.

Individual reports of tyosine kinases

Plants have a massive expansion of the RLK family of TKL kinases, mostly found as transmembrane receptors. Similar to TKLs in other non-animals, some have been shown to have tyrosine kinase activity. The brassinosteroid receptor, BRI1 and it's co-receptor, BAK1 have been shown to autophosphorylate on tyrosine [2, 3].

A peanut MLK kinase was isolated based on its almost stoichiometric level of tyrosine phosphorylation [4], and was shown to autophosphorylate on three tyrosines, including one at the end of the activation loop [5]. Another Arabidopsis MLK kinase, AtSTYPK, was also shown to be a dual-specificity kinase [6].

References

1. Arsova B and Schulze WX. Current status of the plant phosphorylation site database PhosPhAt and its use as a resource for molecular plant physiology. Front Plant Sci. 2012;3:132. DOI:10.3389/fpls.2012.00132 |
2. Oh MH, Clouse SD, and Huber SC. Tyrosine phosphorylation in brassinosteroid signaling. Plant Signal Behav. 2009 Dec;4(12):1182-5. DOI:10.4161/psb.4.12.10046 |
3. Jaillais Y, Hothorn M, Belkhadir Y, Dabi T, Nimchuk ZL, Meyerowitz EM, and Chory J. Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor. Genes Dev. 2011 Feb 1;25(3):232-7. DOI:10.1101/gad.2001911 |
4. Rudrabhatla P and Rajasekharan R. Developmentally regulated dual-specificity kinase from peanut that is induced by abiotic stresses. Plant Physiol. 2002 Sep;130(1):380-90. DOI:10.1104/pp.005173 |
5. Rudrabhatla P and Rajasekharan R. Mutational analysis of stress-responsive peanut dual specificity protein kinase. Identification of tyrosine residues involved in regulation of protein kinase activity. J Biol Chem. 2003 May 9;278(19):17328-35. DOI:10.1074/jbc.M300024200 |
6. Reddy MM and Rajasekharan R. Role of threonine residues in the regulation of manganese-dependent arabidopsis serine/threonine/tyrosine protein kinase activity. Arch Biochem Biophys. 2006 Nov 15;455(2):99-109. DOI:10.1016/j.abb.2006.09.009 |