Neuhäuser, Benjamin ; Dynowski, Marek ; Mayer, Maria ; Ludewig, Uwe (2007):
Regulation of NH4+ transport by essential cross talk between AMT monomers through the carboxyl tails.
In: Plant physiology, 143 (4), pp. 1651-9. ISSN 0032-0889,
[Article]
Abstract
Ammonium transport across plant plasma membranes is facilitated by AMT/Rh-type ammonium transporters (AMTs), which also have homologs in most organisms. In the roots of the plant Arabidopsis (Arabidopsis thaliana), AMTs have been identified that 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 (C terminus) of AMTs, including one that mimics phosphorylation at a putative phosphorylation site, impair NH4+ transport activity. Coexpressing 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 C terminus of one monomer directly contacts the neighboring subunit. It is suggested that part of the cytoplasmic C 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.
Item Type: | Article |
---|---|
Erschienen: | 2007 |
Creators: | Neuhäuser, Benjamin ; Dynowski, Marek ; Mayer, Maria ; Ludewig, Uwe |
Title: | Regulation of NH4+ transport by essential cross talk between AMT monomers through the carboxyl tails |
Language: | English |
Abstract: | Ammonium transport across plant plasma membranes is facilitated by AMT/Rh-type ammonium transporters (AMTs), which also have homologs in most organisms. In the roots of the plant Arabidopsis (Arabidopsis thaliana), AMTs have been identified that 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 (C terminus) of AMTs, including one that mimics phosphorylation at a putative phosphorylation site, impair NH4+ transport activity. Coexpressing 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 C terminus of one monomer directly contacts the neighboring subunit. It is suggested that part of the cytoplasmic C 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. |
Journal or Publication Title: | Plant physiology |
Volume of the journal: | 143 |
Issue Number: | 4 |
Divisions: | 10 Department of Biology > Plant Nutrition and Biomass ?? fb10_botanik ?? 10 Department of Biology |
Date Deposited: | 16 Mar 2010 13:15 |
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