Evidence map›Paper›PMID 25252943›Full record

ArticleDevelopment (Cambridge, England)2014

The conserved LIM domain-containing focal adhesion protein ZYX-1 regulates synapse maintenance in Caenorhabditis elegans.

Shuo Luo, Anneliese M Schaefer, Scott Dour, Michael L Nonet

Open access · greenAbstract read
In one paragraph

Article in Development (Cambridge, England), 2014. 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
0.6field-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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. The actin assembly regulatorbioRxiv : the preprint server for biology · 2025
    Article
  3. Review
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  12. Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  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

4 authors at 1 institution in 1 country.

Shuo LuoDepartment of Anatomy and Neurobiology, Washington University Medical School, 660 S Euclid Ave, St Louis, MO 63110, USA.
Anneliese M SchaeferDepartment of Anatomy and Neurobiology, Washington University Medical School, 660 S Euclid Ave, St Louis, MO 63110, USA Department of Neurology, Washington University Medical School, 660 S Euclid Ave, St Louis, MO 63110, USA.
Scott DourDepartment of Anatomy and Neurobiology, Washington University Medical School, 660 S Euclid Ave, St Louis, MO 63110, USA.
Michael L NonetDepartment of Anatomy and Neurobiology, Washington University Medical School, 660 S Euclid Ave, St Louis, MO 63110, USA nonetm@pcg.wustl.edu.
Washington University in St. Louis · US

Funding

Washington University Center for Translational NeuroscienceP30NS057105 · NINDS · WASHINGTON UNIVERSITY · PI HOLTZMAN, DAVID M. · 2006 to 2011
$8.7M
MOLECULAR GENETIC ANALYSIS OF DEVELOPING SYNAPSESR01NS040094 · NINDS · WASHINGTON UNIVERSITY · PI NONET, MICHAEL L · 2000 to 2018
$4.0M
MOLECULAR GENETIC ANALYSIS OF DEVELOPING SYNAPSESR56NS040094 · NINDS · WASHINGTON UNIVERSITY · PI NONET, MICHAEL L · 2012 to 2012
$380k
NINDS NIH HHS NS040094NINDS NIH HHS NS057105NINDS NIH HHS P30 NS057105NINDS NIH HHS R01 NS040094NINDS NIH HHS R56 NS040094
6 · The paper itself

Abstract

We describe the identification of zyxin as a regulator of synapse maintenance in mechanosensory neurons in C. elegans. zyx-1 mutants lacked PLM mechanosensory synapses as adult animals. However, most PLM synapses initially formed during development but were subsequently lost as the animals developed. Vertebrate zyxin regulates cytoskeletal responses to mechanical stress in culture. Our work provides in vivo evidence in support of such a role for zyxin. In particular, zyx-1 mutant synaptogenesis phenotypes were suppressed by disrupting locomotion of the mutant animals, suggesting that zyx-1 protects mechanosensory synapses from locomotion-induced forces. In cultured cells, zyxin is recruited to focal adhesions and stress fibers via C-terminal LIM domains and modulates cytoskeletal organization via the N-terminal domain. The synapse-stabilizing activity was mediated by a short isoform of ZYX-1 containing only the LIM domains. Consistent with this notion, PLM synaptogenesis was independent of α-actinin and ENA-VASP, both of which bind to the N-terminal domain of zyxin. Our results demonstrate that the LIM domain moiety of zyxin functions autonomously to mediate responses to mechanical stress and provide in vivo evidence for a role of zyxin in neuronal development.

Indexed as

Gene Expression Regulation, DevelopmentalActininAnimalsAnimals, Genetically ModifiedAxonsCaenorhabditis elegansCaenorhabditis elegans ProteinsCarrier ProteinsCytoskeletonFocal AdhesionsMovementMutationNeuronsPhenotypePhosphoproteinsProtein IsoformsActininCaenorhabditis elegans ProteinsCarrier ProteinsPhosphoproteinsProtein IsoformsZYX-1 protein, C elegansZyxinAxon retractionCytoskeletonStress fiberSynaptogenesis

Identifiers

PMID25252943
PMCPMC4197707
OpenAlexW2091689280

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.