Biomaterial Database

NRT2.1 C-terminus phosphorylation prevents root high affinity nitrate uptake activity in Arabidopsis thaliana. 2020

Aurore Jacquot, and Valentin Chaput, and Adeline Mauries, and Zhi Li, and Pascal Tillard, and Cécile Fizames, and Pauline Bonillo, and Fanny Bellegarde, and Edith Laugier, and Véronique Santoni, and Sonia Hem, and Antoine Martin, and Alain Gojon, and Waltraud Schulze, and Laurence Lejay

BPMP, CNRS, INRAE, Institut Agro, Univ Montpellier, 34060, Montpellier, France.

In Arabidopsis thaliana, NRT2.1 codes for a main component of the root nitrate high-affinity transport system. Previous studies revealed that post-translational regulation of NRT2.1 plays an important role in the control of root nitrate uptake and that one mechanism could correspond to NRT2.1 C-terminus processing. To further investigate this hypothesis, we produced transgenic plants with truncated forms of NRT2.1. This revealed an essential sequence for NRT2.1 activity, located between the residues 494 and 513. Using a phospho-proteomic approach, we found that this sequence contains one phosphorylation site, at serine 501, which can inactivate NRT2.1 function when mimicking the constitutive phosphorylation of this residue in transgenic plants. This phenotype could neither be explained by changes in abundance of NRT2.1 and NAR2.1, a partner protein of NRT2.1, nor by a lack of interaction between these two proteins. Finally, the relative level of serine 501 phosphorylation was found to be increased by ammonium nitrate in wild-type plants, leading to the inactivation of NRT2.1 and to a decrease in high affinity nitrate transport into roots. Altogether, these observations reveal a new and essential mechanism for the regulation of NRT2.1 activity.

UI	MeSH Term	Description	Entries
D009566	Nitrates	Inorganic or organic salts and esters of nitric acid. These compounds contain the NO3- radical.	Nitrate
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D010940	Plant Proteins	Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available.	Plant Protein,Protein, Plant,Proteins, Plant
D017360	Arabidopsis	A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.	Arabidopsis thaliana,Cress, Mouse-ear,A. thaliana,A. thalianas,Arabidopses,Arabidopsis thalianas,Cress, Mouse ear,Cresses, Mouse-ear,Mouse-ear Cress,Mouse-ear Cresses,thaliana, A.,thaliana, Arabidopsis,thalianas, A.
D018506	Gene Expression Regulation, Plant	Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.	Plant Gene Expression Regulation,Regulation of Gene Expression, Plant,Regulation, Gene Expression, Plant
D018517	Plant Roots	The usually underground portions of a plant that serve as support, store food, and through which water and mineral nutrients enter the plant. (From American Heritage Dictionary, 1982; Concise Dictionary of Biology, 1990)	Plant Bulbs,Plant Root,Bulb, Plant,Bulbs, Plant,Plant Bulb,Root, Plant,Roots, Plant
D027321	Anion Transport Proteins	Membrane proteins whose primary function is to facilitate the transport of negatively charged molecules (anions) across a biological membrane.	Anion Pumps,ATPHPM,Anion Pump,Anion Transport Proteins (Hepatocyte Plasma Membrane),Pump, Anion,Pumps, Anion
D029681	Arabidopsis Proteins	Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.	Arabidopsis thaliana Proteins,Thale Cress Proteins,Proteins, Arabidopsis thaliana,thaliana Proteins, Arabidopsis
D040901	Proteomics	The systematic study of the complete complement of proteins (PROTEOME) of organisms.	Peptidomics