Evidence map›Paper›PMID 23427270›Full record

ArticleMolecular biology of the cell2013

ZYX-1, the unique zyxin protein of Caenorhabditis elegans, is involved in dystrophin-dependent muscle degeneration.

Claire Lecroisey, Nicolas Brouilly, Hiroshi Qadota, Marie-Christine Mariol, Nicolas C Rochette, Edwige Martin, Guy M Benian, Laurent Ségalat, Nicole Mounier, Kathrin Gieseler

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  9. International journal of molecular sciences · 2021
    Review
  10. Review
  11. Article
  12. Article
  13. Molecular biology of the cell · 2017
    Article
  14. Article
  15. Article
  16. Cellular mechanosensing: getting to the nucleus of it all.Progress in biophysics and molecular biology · 2014
    Review
  17. Review
  18. 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 4 institutions in 2 countries.

Claire LecroiseyUniversité Claude Bernard Lyon 1, 69622 Villeurbanne, France.
Nicolas Brouilly
Hiroshi Qadota
Marie-Christine Mariol
Nicolas C Rochette
Edwige Martin
Guy M Benian
Laurent Ségalat
Nicole Mounier
Kathrin Gieseler
Université Claude Bernard Lyon 1 · FRCentre National de la Recherche Scientifique · FREmory University · USLaboratoire de Biométrie et Biologie Evolutive · FR

Funding

Nematode UNC-98 functions in focal adhensions and nucleiR01AR052133 · NIAMS · EMORY UNIVERSITY · PI BENIAN, GUY MARTIN · 2005 to 2009
$1.2M
NIAMS NIH HHS R01 AR052133NIAMS NIH HHS R01AR052133
6 · The paper itself

Abstract

In vertebrates, zyxin is a LIM-domain protein belonging to a family composed of seven members. We show that the nematode Caenorhabditis elegans has a unique zyxin-like protein, ZYX-1, which is the orthologue of the vertebrate zyxin subfamily composed of zyxin, migfilin, TRIP6, and LPP. The ZYX-1 protein is expressed in the striated body-wall muscles and localizes at dense bodies/Z-discs and M-lines, as well as in the nucleus. In yeast two-hybrid assays ZYX-1 interacts with several known dense body and M-line proteins, including DEB-1 (vinculin) and ATN-1 (α-actinin). ZYX-1 is mainly localized in the middle region of the dense body/Z-disk, overlapping the apical and basal regions containing, respectively, ATN-1 and DEB-1. The localization and dynamics of ZYX-1 at dense bodies depend on the presence of ATN-1. Fluorescence recovery after photobleaching experiments revealed a high mobility of the ZYX-1 protein within muscle cells, in particular at dense bodies and M-lines, indicating a peripheral and dynamic association of ZYX-1 at these muscle adhesion structures. A portion of the ZYX-1 protein shuttles from the cytoplasm into the nucleus, suggesting a role for ZYX-1 in signal transduction. We provide evidence that the zyx-1 gene encodes two different isoforms, ZYX-1a and ZYX-1b, which exhibit different roles in dystrophin-dependent muscle degeneration occurring in a C. elegans model of Duchenne muscular dystrophy.

Indexed as

ActininAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsDystrophinGene ExpressionMolecular Sequence DataMusclesOrgan SpecificityPhylogenyProtein IsoformsProtein TransportSequence Homology, Amino AcidZyxinActininCaenorhabditis elegans ProteinsDystrophinProtein IsoformsZYX-1 protein, C elegansZyxin

Identifiers

PMID23427270
PMCPMC3623643
OpenAlexW2037314385

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.