Evidence map›Paper›PMID 22843664›Full record

ArticlePlant physiology2012

A synthetic approach reveals extensive tunability of auxin signaling.

Kyle A Havens, Jessica M Guseman, Seunghee S Jang, Edith Pierre-Jerome, Nick Bolten, Eric Klavins, Jennifer L Nemhauser

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
17.3field-weighted citation impact, top 1% 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

73 citing papers in PubMed, 139 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Can a plant biologist fix a thermostat?The New phytologist · 2025
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. A single helix repression domain is functional across diverse eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Review
  15. Structural Aspects of Auxin Signaling.Cold Spring Harbor perspectives in biology · 2022
    Review
  16. The Systems and Synthetic Biology of Auxin.Cold Spring Harbor perspectives in biology · 2022
    Review
  17. Review
  18. Article
  19. Repression by theeLife · 2021
    Article
  20. Article

13 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

7 authors at 1 institution in 1 country.

Kyle A HavensDepartment of Electrical Engineering , University of Washington, Seattle, Washington 98195, USA.
Jessica M Guseman
Seunghee S Jang
Edith Pierre-Jerome
Nick Bolten
Eric Klavins
Jennifer L Nemhauser
University of Washington · US

Funding

INTERDISCIPLINARY TRAINING IN DEVELOPMENTAL BIOLOGYT32HD007183 · NICHD · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2015
$5.7M
NICHD NIH HHS T32 HD007183NICHD NIH HHS T32HD007183
6 · The paper itself

Abstract

Explaining how the small molecule auxin triggers diverse yet specific responses is a long-standing challenge in plant biology. An essential step in auxin response is the degradation of Auxin/Indole-3-Acetic Acid (Aux/IAA, referred to hereafter as IAA) repressor proteins through interaction with auxin receptors. To systematically characterize diversity in degradation behaviors among IAA|receptor pairs, we engineered auxin-induced degradation of plant IAA proteins in yeast (Saccharomyces cerevisiae). We found that IAA degradation dynamics vary widely, depending on which receptor is present, and are not encoded solely by the degron-containing domain II. To facilitate this and future studies, we identified a mathematical model able to quantitatively describe IAA degradation behavior in a single parameter. Together, our results demonstrate the remarkable tunability conferred by specific configurations of the auxin response pathway.

Indexed as

Signal TransductionArabidopsisArabidopsis ProteinsF-Box ProteinsFlow CytometryHalf-LifeIndoleacetic AcidsModels, BiologicalPlant Growth RegulatorsPlants, Genetically ModifiedProtein Structure, TertiaryProteolysisReceptors, Cell SurfaceRepressor ProteinsSaccharomyces cerevisiaeSpecies SpecificityArabidopsis ProteinsF-Box Proteinsindoleacetic acidIndoleacetic AcidsPlant Growth RegulatorsReceptors, Cell SurfaceRepressor ProteinsTIR1 protein, Arabidopsis

Identifiers

PMID22843664
PMCPMC3440190
OpenAlexW2079042867

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.