Evidence map›Paper›PMID 15486104›Full record

ArticleThe Plant cell2004

Structure-function analysis of the presumptive Arabidopsis auxin permease AUX1.

Ranjan Swarup, Joanna Kargul, Alan Marchant, Daniel Zadik, Abidur Rahman, Rebecca Mills, Anthony Yemm, Sean May, Lorraine Williams, Paul Millner and 5 more

Abstract read
In one paragraph

Article in The Plant cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 170 papers.

0numbers the graph read from it
0cells of the map it votes in
170citing papers in PubMed
–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

170 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Structural basis of auxin binding and transport byProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. ThePlants (Basel, Switzerland) · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. CUC/auxin patterning of decanalised petal number inQuantitative plant biology · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Visualizing Orientation and Topology of ER Membrane Proteins In Planta.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

110 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors.

Ranjan SwarupSchool of Biosciences, Sutton Bonington Campus, University of Nottingham, United Kingdom.
Joanna Kargul
Alan Marchant
Daniel Zadik
Abidur Rahman
Rebecca Mills
Anthony Yemm
Sean May
Lorraine Williams
Paul Millner
Seiji Tsurumi
Ian Moore
Richard Napier
Ian D Kerr
Malcolm J Bennett

Funding

Biotechnology and Biological Sciences Research Council BBS/B/1356XBiotechnology and Biological Sciences Research Council G17764Biotechnology and Biological Sciences Research Council G18881Biotechnology and Biological Sciences Research Council REI20537Biotechnology and Biological Sciences Research Council REI20541
6 · The paper itself

Abstract

We have investigated the subcellular localization, the domain topology, and the amino acid residues that are critical for the function of the presumptive Arabidopsis thaliana auxin influx carrier AUX1. Biochemical fractionation experiments and confocal studies using an N-terminal yellow fluorescent protein (YFP) fusion observed that AUX1 colocalized with plasma membrane (PM) markers. Because of its PM localization, we were able to take advantage of the steep pH gradient that exists across the plant cell PM to investigate AUX1 topology using YFP as a pH-sensitive probe. The YFP-coding sequence was inserted in selected AUX1 hydrophilic loops to orient surface domains on either apoplastic or cytoplasmic faces of the PM based on the absence or presence of YFP fluorescence, respectively. We were able to demonstrate in conjunction with helix prediction programs that AUX1 represents a polytopic membrane protein composed of 11 transmembrane spanning domains. In parallel, a large aux1 allelic series containing null, partial-loss-of-function, and conditional mutations was characterized to identify the functionally important domains and amino acid residues within the AUX1 polypeptide. Whereas almost all partial-loss-of-function and null alleles cluster in the core permease region, the sole conditional allele aux1-7 modifies the function of the external C-terminal domain.

Indexed as

AllelesAmino Acid SequenceArabidopsisArabidopsis ProteinsCell MembraneGravitropismIndoleacetic AcidsMolecular Sequence DataMutation, MissensePlants, Genetically ModifiedProtein Structure, TertiaryStructure-Activity RelationshipArabidopsis ProteinsAUX1 protein, ArabidopsisIndoleacetic Acids

Identifiers

PMID15486104
PMCPMC527199

What OpenQuestion holds

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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.