Evidence map›Paper›PMID 24572362›Full record

ArticleNature2014

Crystal structure of the plant dual-affinity nitrate transporter NRT1.1.

Ji Sun, John R Bankston, Jian Payandeh, Thomas R Hinds, William N Zagotta, Ning Zheng

Abstract read
In one paragraph

Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
157citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

157 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  3. Identification and characterization ofHorticulture research · 2026
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97 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Ji SunDepartment of Pharmacology, Box 357280, University of Washington, Seattle, Washington 98195, USA.
John R BankstonDepartment of Physiology and Biophysics, Box 357290, University of Washington, Seattle, Washington 98195, USA.
Jian Payandeh1] Department of Pharmacology, Box 357280, University of Washington, Seattle, Washington 98195, USA [2] Department of Structural Biology, Genentech Inc., South San Francisco, California 94080, USA.
Thomas R HindsDepartment of Pharmacology, Box 357280, University of Washington, Seattle, Washington 98195, USA.
William N ZagottaDepartment of Physiology and Biophysics, Box 357290, University of Washington, Seattle, Washington 98195, USA.
Ning Zheng1] Department of Pharmacology, Box 357280, University of Washington, Seattle, Washington 98195, USA [2] Howard Hughes Medical Institute, Box 357280, University of Washington, Seattle, Washington 98195, USA.

Funding

GATING MECHANISMS OF RETINAL ROD CGMP-ACTIVATED CHANNELSR01EY010329 · NEI · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 1994 to 2023
$7.7M
Mechanisms of HCN regulation by accessory subunit Trip8b using fluorescence and eF32NS074545 · NINDS · UNIVERSITY OF WASHINGTON · PI BANKSTON, JOHN · 2011 to 2013
$159k
Howard Hughes Medical InstituteNEI NIH HHS R01 EY010329NEI NIH HHS R01EY10329NINDS NIH HHS F32 NS074545NINDS NIH HHS NS074545
6 · The paper itself

Abstract

Nitrate is a primary nutrient for plant growth, but its levels in soil can fluctuate by several orders of magnitude. Previous studies have identified Arabidopsis NRT1.1 as a dual-affinity nitrate transporter that can take up nitrate over a wide range of concentrations. The mode of action of NRT1.1 is controlled by phosphorylation of a key residue, Thr 101; however, how this post-translational modification switches the transporter between two affinity states remains unclear. Here we report the crystal structure of unphosphorylated NRT1.1, which reveals an unexpected homodimer in the inward-facing conformation. In this low-affinity state, the Thr 101 phosphorylation site is embedded in a pocket immediately adjacent to the dimer interface, linking the phosphorylation status of the transporter to its oligomeric state. Using a cell-based fluorescence resonance energy transfer assay, we show that functional NRT1.1 dimerizes in the cell membrane and that the phosphomimetic mutation of Thr 101 converts the protein into a monophasic high-affinity transporter by structurally decoupling the dimer. Together with analyses of the substrate transport tunnel, our results establish a phosphorylation-controlled dimerization switch that allows NRT1.1 to uptake nitrate with two distinct affinity modes.

Indexed as

Protein MultimerizationAmino Acid SequenceAnion Transport ProteinsArabidopsisBinding SitesBiological TransportCell MembraneCrystallography, X-RayFluorescence Resonance Energy TransferModels, BiologicalModels, MolecularMolecular Sequence DataMutationNitratesNitrate TransportersPhosphorylationAnion Transport ProteinsNitratesNitrate TransportersNRT1.1 protein, ArabidopsisPhosphothreoninePlant ProteinsProtons

Identifiers

PMID24572362
PMCPMC3968801

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.