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

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

© 2020 The Authors. New Phytologist © 2020 New Phytologist Trust.

Détails bibliographiques
Publié dans:The New phytologist. - 1984. - 228(2020), 3 vom: 07. Nov., Seite 1038-1054
Auteur principal: Jacquot, Aurore (Auteur)
Autres auteurs: Chaput, Valentin, Mauries, Adeline, Li, Zhi, Tillard, Pascal, Fizames, Cécile, Bonillo, Pauline, Bellegarde, Fanny, Laugier, Edith, Santoni, Véronique, Hem, Sonia, Martin, Antoine, Gojon, Alain, Schulze, Waltraud, Lejay, Laurence
Format: Article en ligne
Langue:English
Publié: 2020
Accès à la collection:The New phytologist
Sujets:Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana NRT2.1 nitrate transporter phosphorylation posttranslational regulation root nitrate uptake Anion Transport Proteins Arabidopsis Proteins plus... AtNRT2.1 protein, Arabidopsis Nitrates Plant Proteins
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500 |a CommentIn: New Phytol. 2020 Nov;228(3):802-804. doi: 10.1111/nph.16803. - PMID 32767375 
500 |a Citation Status MEDLINE 
520 |a © 2020 The Authors. New Phytologist © 2020 New Phytologist Trust. 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Arabidopsis thaliana 
650 4 |a NRT2.1 
650 4 |a nitrate transporter 
650 4 |a phosphorylation 
650 4 |a posttranslational regulation 
650 4 |a root nitrate uptake 
650 7 |a Anion Transport Proteins  |2 NLM 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a AtNRT2.1 protein, Arabidopsis  |2 NLM 
650 7 |a Nitrates  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
700 1 |a Chaput, Valentin  |e verfasserin  |4 aut 
700 1 |a Mauries, Adeline  |e verfasserin  |4 aut 
700 1 |a Li, Zhi  |e verfasserin  |4 aut 
700 1 |a Tillard, Pascal  |e verfasserin  |4 aut 
700 1 |a Fizames, Cécile  |e verfasserin  |4 aut 
700 1 |a Bonillo, Pauline  |e verfasserin  |4 aut 
700 1 |a Bellegarde, Fanny  |e verfasserin  |4 aut 
700 1 |a Laugier, Edith  |e verfasserin  |4 aut 
700 1 |a Santoni, Véronique  |e verfasserin  |4 aut 
700 1 |a Hem, Sonia  |e verfasserin  |4 aut 
700 1 |a Martin, Antoine  |e verfasserin  |4 aut 
700 1 |a Gojon, Alain  |e verfasserin  |4 aut 
700 1 |a Schulze, Waltraud  |e verfasserin  |4 aut 
700 1 |a Lejay, Laurence  |e verfasserin  |4 aut 
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