Evidence map›Paper›PMID 22510987›Full record

ArticleDevelopment (Cambridge, England)2012

The novel intestinal filament organizer IFO-1 contributes to epithelial integrity in concert with ERM-1 and DLG-1.

Katrin Carberry, Tobias Wiesenfahrt, Florian Geisler, Stephanie Stöcker, Harald Gerhardus, Daniel Überbach, Wayne Davis, Erik Jorgensen, Rudolf E Leube, Olaf Bossinger

Open access · bronzeAbstract read
In one paragraph

Article in Development (Cambridge, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.7field-weighted citation impact, top 38% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Epithelial morphogenesis, tubulogenesis and forces in organogenesis.Current topics in developmental biology · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Intracellular Motility of Intermediate Filaments.Cold Spring Harbor perspectives in biology · 2017
    Review
  12. Article
  13. Article
  14. New insights into estrogenic regulation ofJournal of biomedical research · 2016
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. The minus-end actin capping protein, UNC-94/tropomodulin, regulates development of the Caenorhabditis elegans intestine.Developmental dynamics : an official publication of the American Association of Anatomists · 2014
    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

10 authors at 3 institutions in 2 countries.

Katrin CarberryInstitute of Molecular and Cellular Anatomy (MOCA), RWTH Aachen University, D-52074 Aachen, Germany.
Tobias Wiesenfahrt
Florian Geisler
Stephanie Stöcker
Harald Gerhardus
Daniel Überbach
Wayne Davis
Erik Jorgensen
Rudolf E Leube
Olaf Bossinger
RWTH Aachen University · DEHoward Hughes Medical Institute · USUniversity of Utah · US

Funding

SYNAPTIC FUNCTION IN THE NEMATODE C. ELEGANSR01NS034307 · NINDS · UNIVERSITY OF UTAH · PI JORGENSEN, ERIK M · 1995 to 2024
$5.8M
NINDS NIH HHS R01 NS034307
6 · The paper itself

Abstract

The nematode Caenorhabditis elegans is an excellent model system in which to study in vivo organization and function of the intermediate filament (IF) system for epithelial development and function. Using a transgenic ifb-2::cfp reporter strain, a mutagenesis screen was performed to identify mutants with aberrant expression patterns of the IF protein IFB-2, which is expressed in a dense network at the subapical endotube just below the microvillar brush border of intestinal cells. Two of the isolated alleles (kc2 and kc3) were mapped to the same gene, which we refer to as ifo-1 (intestinal filament organizer). The encoded polypeptide colocalizes with IF proteins and F-actin in the intestine. The apical localization of IFO-1 does not rely on IFB-2 but is dependent on LET-413, a basolateral protein involved in apical junction assembly and maintenance of cell polarity. In mutant worms, IFB-2 and IFC-2 are mislocalized in cytoplasmic granules and accumulate in large aggregates at the C. elegans apical junction (CeAJ) in a DLG-1-dependent fashion. Electron microscopy reveals loss of the prominent endotube and disordered but still intact microvilli. Semiquantitative fluorescence microscopy revealed a significant decrease of F-actin, suggesting a general role of IFO-1 in cytoskeletal organization. Furthermore, downregulation of the cytoskeletal organizer ERM-1 and the adherens junction component DLG-1, each of which leads to F-actin reduction on its own, induces a novel synthetic phenotype in ifo-1 mutants resulting in disruption of the lumen. We conclude that IFO-1 is a multipurpose linker between different cytoskeletal components of the C. elegans intestinal terminal web and contributes to proper epithelial tube formation.

Indexed as

ActinsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCytoskeletal ProteinsCytoskeletonGuanylate KinasesIntermediate FilamentsActinsCaenorhabditis elegans ProteinsCytoskeletal ProteinsDLG-1 protein, C elegansERM-1 protein, C elegansGuanylate Kinases

Identifiers

PMID22510987
PMCPMC4074299
OpenAlexW2030067938

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.