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Published on March 2, 2007; 10.1104/pp.106.094243

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Received December 5, 2006
Accepted February 22, 2007

Regulation of NH4+ Transport by Essential Cross-talk between AMT Monomers through the Carboxyl-tails

Benjamin Neuhäuser , Marek Dynowski , Maria Mayer , and Uwe Ludewig *

Zentrum für Molekularbiologie der Pflanzen (ZMBP), Pflanzenphysiologie, Universität Tübingen, Auf der Morgenstelle 1, D-72076 Tübingen, Germany

* Corresponding author; email: uwe.ludewig{at}zmbp.uni-tuebingen.de.

The ammonium transport across plant plasma membranes is facilitated by AMT/Rh-type ammonium transporters, which have homologs also in most organisms. In the root of the plant Arabidopsis thaliana, AMTs have been identified which function directly in the high affinity NH4+ acquisition from soil. Here we show that AtAMT1;2 has a distinct role, as it is located in the plasma membrane of the root endodermis. AtAMT1;2 functions as a comparatively low affinity NH4+ transporter. Mutations at the highly conserved carboxyl-terminus of AMTs, including one that mimics phosphorylation at a putative phosphorylation site, impair NH4+ transport activity. Co-expressing these mutants along with wild type AtAMT1;2 substantially reduced the activity of the wild type transporter. A molecular model of AtAMT1;2 provides a plausible explanation for the dominant inhibition, as the carboxyl-terminus of one monomer directly contacts the neighboring subunit. It is suggested that part of the cytoplasmic carboxyl-terminus of a single monomer can gate the AMT trimer. This regulatory mechanism for rapid and efficient inactivation of NH4+ transporters may apply to several AMT members to prevent excess influx of cytotoxic ammonium.




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