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Immunolocalization of Dually Phosphorylated MAPKs in Dividing Root Meristem Cells of Vicia Faba, Pisum Sativum, Lupinus Luteus and Lycopersicon Esculentum

Overview
Journal Plant Cell Rep
Publisher Springer
Date 2015 Feb 6
PMID 25652240
Citations 2
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Abstract

In plants, phosphorylated MAPKs display constitutive nuclear localization; however, not all studied plant species show co-localization of activated MAPKs to mitotic microtubules. The mitogen-activated protein kinase (MAPK) signaling pathway is involved not only in the cellular response to biotic and abiotic stress but also in the regulation of cell cycle and plant development. The role of MAPKs in the formation of a mitotic spindle has been widely studied and the MAPK signaling pathway was found to be indispensable for the unperturbed course of cell division. Here we show cellular localization of activated MAPKs (dually phosphorylated at their TXY motifs) in both interphase and mitotic root meristem cells of Lupinus luteus, Pisum sativum, Vicia faba (Fabaceae) and Lycopersicon esculentum (Solanaceae). Nuclear localization of activated MAPKs has been found in all species. Co-localization of these kinases to mitotic microtubules was most evident in L. esculentum, while only about 50% of mitotic cells in the root meristems of P. sativum and V. faba displayed activated MAPKs localized to microtubules during mitosis. Unexpectedly, no evident immunofluorescence signals at spindle microtubules and phragmoplast were noted in L. luteus. Considering immunocytochemical analyses and studies on the impact of FR180204 (an inhibitor of animal ERK1/2) on mitotic cells, we hypothesize that MAPKs may not play prominent role in the regulation of microtubule dynamics in all plant species.

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References
1.
Liu X, Yan S, Zhou T, Terada Y, Erikson R . The MAP kinase pathway is required for entry into mitosis and cell survival. Oncogene. 2004; 23(3):763-76. DOI: 10.1038/sj.onc.1207188. View

2.
Fernandez-Pascual M, Lucas M, de Felipe M, Bosca L, Hirt H, Golvano M . Involvement of mitogen-activated protein kinases in the symbiosis Bradyrhizobium-Lupinus. J Exp Bot. 2006; 57(11):2735-42. DOI: 10.1093/jxb/erl038. View

3.
Ovecka M, Takac T, Komis G, Vadovic P, Bekesova S, Doskocilova A . Salt-induced subcellular kinase relocation and seedling susceptibility caused by overexpression of Medicago SIMKK in Arabidopsis. J Exp Bot. 2014; 65(9):2335-50. PMC: 4036504. DOI: 10.1093/jxb/eru115. View

4.
Perrett R, Fowkes R, Caunt C, Tsaneva-Atanasova K, Bowsher C, McArdle C . Signaling to extracellular signal-regulated kinase from ErbB1 kinase and protein kinase C: feedback, heterogeneity, and gating. J Biol Chem. 2013; 288(29):21001-21014. PMC: 3774369. DOI: 10.1074/jbc.M113.455345. View

5.
Kong F, Wang J, Cheng L, Liu S, Wu J, Peng Z . Genome-wide analysis of the mitogen-activated protein kinase gene family in Solanum lycopersicum. Gene. 2012; 499(1):108-20. DOI: 10.1016/j.gene.2012.01.048. View