Evidence map›Paper›PMID 21052782›Full record

ArticlePlant molecular biology2011

ARABIDILLO proteins have a novel and conserved domain structure important for the regulation of their stability.

Cândida Nibau, Daniel J Gibbs, Karen A Bunting, Laura A Moody, Emma J Smiles, Jennifer A Tubby, Susan J Bradshaw, Juliet C Coates

Abstract read
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Article in Plant molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Whole-Genome Sequencing and Analysis of Tumour-Forming Radish (International journal of molecular sciences · 2024
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  8. Article
  9. Comprehensive expression analysis of rice Armadillo gene family during abiotic stress and development.DNA research : an international journal for rapid publication of reports on genes and genomes · 2014
    Article
  10. Article
  11. Article
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  13. 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

8 authors at 3 institutions in 1 country.

Cândida NibauSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.
Daniel J Gibbs
Karen A Bunting
Laura A Moody
Emma J Smiles
Jennifer A Tubby
Susan J Bradshaw
Juliet C Coates
University of Birmingham · GBQueen's Medical Centre · GBUniversity of Nottingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/007750/1Biotechnology and Biological Sciences Research Council BB/D007550/1Wellcome Trust
6 · The paper itself

Abstract

ARABIDILLO proteins are F-box-Armadillo (ARM) proteins that regulate root branching in Arabidopsis. Many F-box proteins in plants, yeast and mammals are unstable. In plants, the mechanism for this instability has not been fully investigated. Here, we show that a conserved family of plant ARABIDILLO-related proteins has a unique domain structure consisting of an F-box and leucine-rich repeats (LRRs) followed by ARM-repeats. The LRRs are similar to those found in other plant and animal F-box proteins, including cell cycle proteins and hormone receptors. We demonstrate that the LRRs are required for ARABIDILLO1 function in vivo. ARABIDILLO1 protein is unstable: we show that ARABIDILLO1 protein is associated with ubiquitin and is turned over by the proteasome. Both the F-box and LRR regions of ARABIDILLO1 appear to enable this turnover to occur. Application of known lateral root-regulating signals has no effect on ARABIDILLO1 stability. In addition, plants that lack or overexpress ARABIDILLO proteins respond normally to known lateral root-regulating signals. Thus, we suggest that the signal(s) regulating ARABIDILLO stability in vivo may be either highly specific or novel. The structural conservation between ARABIDILLOs and other plant and animal F-box proteins suggests that the stability of other F-box proteins may be controlled by similar mechanisms.

Indexed as

Amino Acid SequenceArabidopsis Proteinsbeta CateninBinding SitesBlotting, WesternConserved SequenceF-Box ProteinsGene Expression Regulation, PlantModels, MolecularMolecular Sequence DataMutationPhylogenyProteasome Endopeptidase ComplexProtein BindingProtein StabilityProtein Structure, Tertiaryarabidillo-1 protein, ArabidopsisArabidopsis ProteinsASK1 protein, ArabidopsisASK2 protein, Arabidopsisbeta CateninF-Box ProteinsProteasome Endopeptidase ComplexSKP Cullin F-Box Protein LigasesUbiquitin

Identifiers

PMID21052782
OpenAlexW2001618528

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.