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• W3130353233 endingPage "1812" @default.
• W3130353233 startingPage "1790" @default.
• W3130353233 abstract "Abstract Calcium (Ca2+)/calmodulin (CaM)-dependent protein kinase (CCaMK) is an important positive regulator of abscisic acid (ABA) and abiotic stress signaling in plants and is believed to act upstream of mitogen-activated protein kinase (MAPK) in ABA signaling. However, it is unclear how CCaMK activates MAPK in ABA signaling. Here, we show that OsDMI3, a rice (Oryza sativa) CCaMK, directly interacts with and phosphorylates OsMKK1, a MAPK kinase (MKK) in rice, in vitro and in vivo. OsDMI3 was found to directly phosphorylate Thr-25 in the N-terminus of OsMKK1, and this Thr-25 phosphorylation is OsDMI3-specific in ABA signaling. The activation of OsMKK1 and its downstream kinase OsMPK1 is dependent on Thr-25 phosphorylation of OsMKK1 in ABA signaling. Moreover, ABA treatment induces phosphorylation in the activation loop of OsMKK1, and the two phosphorylations, in the N-terminus and in the activation loop, are independent. Further analyses revealed that OsDMI3-mediated phosphorylation of OsMKK1 positively regulates ABA responses in seed germination, root growth, and tolerance to both water stress and oxidative stress. Our results indicate that OsMKK1 is a direct target of OsDMI3, and OsDMI3-mediated phosphorylation of OsMKK1 plays an important role in activating the MAPK cascade and ABA signaling." @default.
• W3130353233 created "2021-03-01" @default.
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• W3130353233 date "2021-02-25" @default.
• W3130353233 modified "2023-10-14" @default.
• W3130353233 title "Rice calcium/calmodulin-dependent protein kinase directly phosphorylates a mitogen-activated protein kinase kinase to regulate abscisic acid responses" @default.
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• W3130353233 doi "https://doi.org/10.1093/plcell/koab071" @default.
• W3130353233 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8254507" @default.
• W3130353233 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33630095" @default.
• W3130353233 hasPublicationYear "2021" @default.
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