Evidence map›Paper›PMID 19019987›Full record

ArticleMolecular biology of the cell2009

Mutations in the Arabidopsis peroxisomal ABC transporter COMATOSE allow differentiation between multiple functions in planta: insights from an allelic series.

Daniela Dietrich, Heike Schmuths, Carine De Marcos Lousa, Jocelyn M Baldwin, Stephen A Baldwin, Alison Baker, Frederica L Theodoulou, Michael J Holdsworth

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Plant peroxisomal solute transporter proteins.Journal of integrative plant biology · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Peroxisomal ABC transporters: functions and mechanism.Biochemical Society transactions · 2015
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Acyl-lipid metabolism.The arabidopsis book · 2013
    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

8 authors at 3 institutions in 1 country.

Daniela DietrichDepartment of Plant and Crop Sciences, School of Biosciences, University of Nottingham, Sutton Bonington Campus, Loughborough, United Kingdom.
Heike Schmuths
Carine De Marcos Lousa
Jocelyn M Baldwin
Stephen A Baldwin
Alison Baker
Frederica L Theodoulou
Michael J Holdsworth
University of Leeds · GBUniversity of Nottingham · GBRothamsted Research · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F007108/1Biotechnology and Biological Sciences Research Council BB/F007299/1Biotechnology and Biological Sciences Research Council BBS/E/C/00004948Biotechnology and Biological Sciences Research Council P19769Biotechnology and Biological Sciences Research Council P19770
6 · The paper itself

Abstract

COMATOSE (CTS), the Arabidopsis homologue of human Adrenoleukodystrophy protein (ALDP), is required for import of substrates for peroxisomal beta-oxidation. A new allelic series and a homology model based on the bacterial ABC transporter, Sav1866, provide novel insights into structure-function relations of ABC subfamily D proteins. In contrast to ALDP, where the majority of mutations result in protein absence from the peroxisomal membrane, all CTS mutants produced stable protein. Mutation of conserved residues in the Walker A and B motifs in CTS nucleotide-binding domain (NBD) 1 resulted in a null phenotype but had little effect in NBD2, indicating that the NBDs are functionally distinct in vivo. Two alleles containing mutations in NBD1 outside the Walker motifs (E617K and C631Y) exhibited resistance to auxin precursors 2,4-dichlorophenoxybutyric acid (2,4-DB) and indole butyric acid (IBA) but were wild type in all other tests. The homology model predicted that the transmission interfaces are domain-swapped in CTS, and the differential effects of mutations in the conserved "EAA motif" of coupling helix 2 supported this prediction, consistent with distinct roles for each NBD. Our findings demonstrate that CTS functions can be separated by mutagenesis and the structural model provides a framework for interpretation of phenotypic data.

Indexed as

AllelesArabidopsisMutationAdenosine TriphosphatasesAmino Acid SequenceAnimalsArabidopsis ProteinsATP-Binding Cassette TransportersCatalytic DomainFatty Acid Transport ProteinsHumansIndoleacetic AcidsModels, MolecularMolecular Sequence DataPeroxisomesPhenotypeAdenosine TriphosphatasesArabidopsis ProteinsAt4g39850 protein, ArabidopsisATP-Binding Cassette TransportersFatty Acid Transport ProteinsIndoleacetic AcidsSucrose

Identifiers

PMID19019987
PMCPMC2613106
OpenAlexW2141142106

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.