Phosphorylation by CIPK23 regulates the high-affinity Mn transporter NRAMP1 in Arabidopsis.

Thibault Kosuth, Alexandra Leskova, Reyes Ródenas, Gregory Vert, Catherine Curie, Loren Castaings

FEBS letters 2023 Aug

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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. © 2023 Federation of European Biochemical Societies.

Citation

Thibault Kosuth, Alexandra Leskova, Reyes Ródenas, Gregory Vert, Catherine Curie, Loren Castaings. Phosphorylation by CIPK23 regulates the high-affinity Mn transporter NRAMP1 in Arabidopsis. FEBS letters. 2023 Aug;597(16):2048-2058