title: Feedback inhibition of ammonium uptake by a phospho-dependent allosteric mechanism in Arabidopsis.
abstract: The acquisition of nutrients requires tight regulation to ensure optimal supply while preventing accumulation to toxic levels. Ammonium transporter/methylamine permease/rhesus (AMT/Mep/Rh) transporters are responsible for ammonium acquisition in bacteria, fungi, and plants. The ammonium transporter AMT1;1 from Arabidopsis thaliana uses a novel regulatory mechanism requiring the productive interaction between a trimer of subunits for function. Allosteric regulation is mediated by a cytosolic C-terminal trans-activation domain, which carries a conserved Thr (T460) in a critical position in the hinge region of the C terminus. When expressed in yeast, mutation of T460 leads to inactivation of the trimeric complex. This study shows that phosphorylation of T460 is triggered by ammonium in a time- and concentration-dependent manner. Neither Gln nor l-methionine sulfoximine-induced ammonium accumulation were effective in inducing phosphorylation, suggesting that roots use either the ammonium transporter itself or another extracellular sensor to measure ammonium concentrations in the rhizosphere. Phosphorylation of T460 in response to an increase in external ammonium correlates with inhibition of ammonium uptake into Arabidopsis roots. Thus, phosphorylation appears to function in a feedback loop restricting ammonium uptake. This novel autoregulatory mechanism is capable of tuning uptake capacity over a wide range of supply levels using an extracellular sensory system, potentially mediated by a transceptor (i.e., transporter and receptor).
authors: Department of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.
authors: Viviane
authors: V
authors: Lanquar
authors: Dominique
authors: D
authors: Loqué
authors: Friederike
authors: F
authors: Hörmann
authors: Lixing
authors: L
authors: Yuan
authors: Anne
authors: A
authors: Bohner
authors: Wolfgang R
authors: WR
authors: Engelsberger
authors: Sylvie
authors: S
authors: Lalonde
authors: Waltraud X
authors: WX
authors: Schulze
authors: Nicolaus
authors: N
authors: von Wirén
authors: Wolf B
authors: WB
authors: Frommer
mesh_terms: D000494:Allosteric Regulation / Q000502:physiology; D000595:Amino Acid Sequence / Q000502:physiology; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D017660:Autoreceptors / Q000378:metabolism; D027682:Cation Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D017124:Conserved Sequence / Q000502:physiology; D025461:Feedback, Physiological / Q000502:physiology*; D006706:Homeostasis / Q000502:physiology; D010758:Phosphorus / Q000378:metabolism*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D018517:Plant Roots / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000502:physiology; D021122:Protein Subunits / Q000378:metabolism; D000644:Quaternary Ammonium Compounds / Q000378:metabolism*; D013912:Threonine / Q000378:metabolism; D013997:Time Factors
chemical_list: D017660:Autoreceptors; D027682:Cation Transport Proteins; D010940:Plant Proteins; D021122:Protein Subunits; D000644:Quaternary Ammonium Compounds; C088952:ammonium transporters, plant; D010758:Phosphorus; D013912:Threonine; D010770:Phosphotransferases