TU Darmstadt / ULB / TUbiblio

Regulation of NH4+ transport by essential cross talk between AMT monomers through the carboxyl tails

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
PPN:
Export:
Suche nach Titel in: TUfind oder in Google
Send an inquiry Send an inquiry

Options (only for editors)
Show editorial Details Show editorial Details