ArticleJournal of experimental botany2024
Phosphoregulation in the N-terminus of NRT2.1 affects nitrate uptake by controlling the interaction of NRT2.1 with NAR2.1 and kinase HPCAL1 in Arabidopsis.
Article in Journal of experimental botany, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 16 citations in OpenAlex.
- Expansion and Nitrate-Responsive Expression of NRT3 Transport Regulators in Maritime Pine.Plants (Basel, Switzerland) · 2026Article
- SaNAR2.2, A Novel Member of the NAR2 Family from the EuhalophyteMembranes · 2026Article
- Homeostasis of ammonium and nitrate in plants.Quantitative plant biology · 2026Review
- Rapeseed transcription factor BnaC9bHLH35 promotes root growth and improves nitrogen use efficiency under low nitrate conditions.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Quantitative Proteomic Analysis of Brassica Napus Reveals Intersections Between Nutrient Deficiency Responses.Plant, cell & environment · 2025Article
- Genome-wide identification of high-affinity nitrate transporter 2 (NRT2) gene family under phytohormones and abiotic stresses in alfalfa (Medicago sativa).Scientific reports · 2024Article
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9 authors at 2 institutions in 2 countries.
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Abstract
NRT2.1, the major high affinity nitrate transporter in roots, can be phosphorylated at five different sites within the N- and the C-terminus. Here, we characterized the functional relationship of two N-terminal phosphorylation sites, S21 and S28, in Arabidopsis. Based on a site-specific correlation network, we identified a receptor kinase (HPCAL1, AT5G49770), phosphorylating NRT2.1 at S21 and resulting in active nitrate uptake. HPCAL1 itself was regulated by phosphorylation at S839 and S870 within its kinase domain. In the active state, when S839 was dephosphorylated and S870 was phosphorylated, HPCAL1 was found to interact with the N-terminus of NRT2.1, mainly when S28 was dephosphorylated. Phosphorylation of NRT2.1 at S21 resulted in a reduced interaction of NRT2.1 with its activator NAR2.1, but nitrate transport activity remained. By contrast, phosphorylated NRT2.1 at S28 enhanced the interaction with NAR2.1, but reduced the interaction with HPCAL1. Here we identified HPCAL1 as the kinase affecting this phospho-switch through phosphorylation of NRT2.1 at S21.
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