Adjusting ammonium uptake via phosphorylation


In plants, AMT/MEP/Rh superfamily mediates high affinity ammonium uptake. AMT/MEP transporters form a trimeric complex, which requires a productive interaction between subunits in order to be functional. The AMT/MEP C-terminal domain is highly conserved in more than 700 AMT homologs from cyanobacteria to higher plants with no cases found to be lacking this domain. AMT1;1 exists in active and inactive states, probably controlled by the spatial positioning of the C-terminus. Ammonium triggers the phosphorylation of a conserved threonine residue (T460) in the C-terminus of AMT1;1 in a time- and concentration-dependent manner. The T460 phosphorylation level correlates with a decrease of root ammonium uptake. We propose that ammonium-induced phosphorylation modulates ammonium uptake as a general mechanism to protect against ammonium toxicity.

 Article Addendum to:

V Lanquar, D Loqué, F Hörmann, L Yuan, A Bohner, WR Engelsberger, S Lalonde, WX Schulze, Wirén N von, WB Frommer. Feedback inhibition of ammonium uptake by a phospho-dependent allosteric mechanism in Arabidopsis. Plant Cell 2009; 21: 3610- 22.
PMID: 19948793 DOI: 10.1105/tpc.109.068593

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Adjusting ammonium uptake via phosphorylation