Phosphoproteomic analysis reveals that dehydrins ERD10 and ERD14 are phosphorylated by SNF1‐related protein kinase 2.10 in response to osmotic stress. (10th December 2018)

• Record Type: Journal Article
• Authors: Maszkowska, Justyna; Dębski, Janusz; Kulik, Anna; Kistowski, Michał; Bucholc, Maria; Lichocka, Małgorzata; Klimecka, Maria; Sztatelman, Olga; Szymańska, Katarzyna Patrycja; Dadlez, Michał; Dobrowolska, Grażyna
• Is Part Of: Plant, cell and environment. Volume 42:Number 3(2019)
• Page Start: 931
• Page End: 946
• Publication Date: 2018-12-10
• Subjects: Plant physiology -- Periodicals; Plant cells and tissues -- Periodicals; Plant communities -- Periodicals; 581.105
• DOI: 10.1111/pce.13465
• Languages: English
• ISSNs: 0140-7791

Abstract

Abstract: SNF1‐related protein kinases 2 (SnRK2s) regulate the plant responses to abiotic stresses, especially water deficits. They are activated in plants subjected to osmotic stress, and some of them are additionally activated in response to enhanced concentrations of abscisic acid (ABA) in plant cells. The SnRK2s that are activated in response to ABA are key elements of ABA signalling that regulate plant acclimation to environmental stresses and ABA‐dependent development. Much less is known about the SnRK2s that are not activated by ABA, albeit several studies have shown that these kinases are also involved in response to osmotic stress. Here, we show that one of the Arabidopsis thaliana ABA‐non‐activated SnRK2s, SnRK2.10, regulates not only the response to salinity but also the plant sensitivity to dehydration. Several potential SnRK2.10 targets phosphorylated in response to stress were identified by a phosphoproteomic approach, including the dehydrins ERD10 and ERD14. Their phosphorylation by SnRK2.10 was confirmed in vitro. Our data suggest that the phosphorylation of ERD14 within the S‐segment is involved in the regulation of dehydrin subcellular localization in response to stress. Abstract : The ABA‐non‐activated SNF1‐related protein kinases 2 (SnRK2s) are strongly activated in the plant response to water deficits and salinity; however, information concerning their roles in the response to stress is limited. Using a phosphoproteomic approach, we identified several potential targets of one kinase of this group, SnRK2.10, that are phosphorylated in response to salt stress. Our data showed that two dehydrins, ERD10 and ERD14, are phosphorylated by SnRK2.10 in vivo and in vitro and suggested that the phosphorylation of ERD14 within the S‐segment is involved in the regulation of its subcellular localization in response to stress.