Evidence map›Paper›PMID 15173569›Full record

ArticlePlant physiology2004

IAR4, a gene required for auxin conjugate sensitivity in Arabidopsis, encodes a pyruvate dehydrogenase E1alpha homolog.

Sherry LeClere, Rebekah A Rampey, Bonnie Bartel

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
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

25 citing papers in PubMed, 46 citations in OpenAlex.

  1. RNA mNature plants · 2025
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Feedback Microtubule Control and Microtubule-Actin Cross-talk inMolecular & cellular proteomics : MCP · 2017
    Article
  15. Article
  16. Article
  17. Auxin biosynthesis and storage forms.Journal of experimental botany · 2013
    Review
  18. Article
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

Sherry LeClereDepartment of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005, USA.
Rebekah A Rampey
Bonnie Bartel
Rice University · US

Funding

BIOTECHNOLOGY RESEARCH TRAINING GRANTT32GM008362 · NIGMS · RICE UNIVERSITY · PI WEST, JENNIFER L · 1990 to 2010
$3.6M
REGULATION OF THE PLANT GROWTH HORMONE INDOLEACETIC ACIDR29GM054749 · NIGMS · RICE UNIVERSITY · PI BARTEL, BONNIE · 1996 to 2000
$129k
NIGMS NIH HHS R29 GM054749NIGMS NIH HHS R29-GM54749NIGMS NIH HHS T32-GM08362
6 · The paper itself

Abstract

The formation and hydrolysis of indole-3-acetic acid (IAA) conjugates represent a potentially important means for plants to regulate IAA levels and thereby auxin responses. The identification and characterization of mutants defective in these processes is advancing the understanding of auxin regulation and response. Here we report the isolation and characterization of the Arabidopsis iar4 mutant, which has reduced sensitivity to several IAA-amino acid conjugates. iar4 is less sensitive to a synthetic auxin and low concentrations of an ethylene precursor but responds to free IAA and other hormones tested similarly to wild type. The gene defective in iar4 encodes a homolog of the E1alpha-subunit of mitochondrial pyruvate dehydrogenase, which converts pyruvate to acetyl-coenzyme A. We did not detect glycolysis or Krebs-cycle-related defects in the iar4 mutant, and a T-DNA insertion in the IAR4 coding sequence conferred similar phenotypes as the originally identified missense allele. In contrast, we found that disruption of the previously described mitochondrial pyruvate dehydrogenase E1alpha-subunit does not alter IAA-Ala responsiveness or confer any obvious phenotypes. It is possible that IAR4 acts in the conversion of indole-3-pyruvate to indole-3-acetyl-coenzyme A, which is a potential precursor of IAA and IAA conjugates.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsIndoleacetic AcidsMitochondriaMolecular Sequence DataMutationPhylogenyPyruvate DecarboxylasePyruvate Dehydrogenase (Lipoamide)Sequence Homology, Amino AcidArabidopsis ProteinsIAR4 protein, Arabidopsisindoleacetic acidIndoleacetic AcidsPyruvate Decarboxylasepyruvate dehydrogenase E1alpha subunitPyruvate Dehydrogenase (Lipoamide)

Identifiers

PMID15173569
PMCPMC514133
OpenAlexW2046411945

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.