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- W4385331037 abstract "Manganese (Mn) is essential for plants but is toxic when taken up in excess. To maintain Mn homeostasis, the root Mn transporter natural resistance associated macrophage protein 1 (NRAMP1) cycles from the plasma membrane to endosomes upon phosphorylation. To identify the kinase involved, a split-luciferase screening was carried out between NRAMP1 and kinases of the CIPK family and identified CIPK23 as a partner of NRAMP1. The interaction was confirmed by split-mCitrine bimolecular fluorescence complementation and co-immunoprecipitation assays. In vitro phosphorylation assays pinpointed two CIPK23 target residues in NRAMP1, among which serine 20, important for endocytosis. Interestingly, Mn-induced internalization of NRAMP1 was unaffected by cipk23 mutation suggesting a potential redundancy between CIPK23 and other kinase(s). How CIPK23 could regulate NRAMP1 in response to Mn availability is discussed." @default.
- W4385331037 created "2023-07-29" @default.
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- W4385331037 date "2023-08-01" @default.
- W4385331037 modified "2023-10-18" @default.
- W4385331037 title "Phosphorylation by <scp>CIPK23</scp> regulates the high‐affinity Mn transporter <scp>NRAMP1</scp> in <i>Arabidopsis</i>" @default.
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- W4385331037 doi "https://doi.org/10.1002/1873-3468.14706" @default.
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