Evidence map›Paper›PMID 23638401›Full record

ArticlePeerJ2013

Mutations changing tropomodulin affinity for tropomyosin alter neurite formation and extension.

Natalia Moroz, Laurent Guillaud, Brinda Desai, Alla S Kostyukova

Open access · goldAbstract read
In one paragraph

Article in PeerJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Structural insights into the tropomodulin assembly at the pointed ends of actin filaments.Protein science : a publication of the Protein Society · 2021
    Article
  4. Tropomodulin Isoform-Specific Regulation of Dendrite Development and Synapse Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Tropomodulins and tropomyosins: working as a team.Journal of muscle research and cell motility · 2013
    Review
  14. Review
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 3 institutions in 2 countries.

Natalia Moroz *Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, USA.
Laurent Guillaud *Cellular and Molecular Synaptic Function Unit, Okinawa Institute of Science and Technology - Graduate University, Kunigami, Okinawa, Japan.
Brinda DesaiDepartment of Neuroscience and Cell Biology, Robert Wood Johnson Medical School, Piscataway, NJ, USA.
Alla S KostyukovaVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, USA.
Johnson University · USOkinawa Institute of Science and Technology Graduate University · JPWashington State University · US

Funding

Factors influencing regulation of the dynamics of the actin filament pointed endR01GM081688 · NIGMS · WASHINGTON STATE UNIVERSITY · PI KOSTYUKOVA, ALLA S. · 2009 to 2013
$1.6M
NIGMS NIH HHS R01 GM081688
6 · The paper itself

Abstract

Assembly of the actin cytoskeleton is an important part of formation of neurites in developing neurons. Tropomodulin, a tropomyosin-dependent capping protein for the pointed end of the actin filament, is one of the key players in this process. Tropomodulin binds tropomyosin in two binding sites. Tmod1 and Tmod2, tropomodulin isoforms found in neurons, were overexpressed in PC12 cells, a model system for neuronal differentiation. Tmod1 did not affect neuronal differentiation; while cells expressing Tmod2 showed a significant reduction in the number and the length of neurites. Both tropomodulins bind short α-, γ- and δ-tropomyosin isoforms. Mutations in one of the tropomyosin-binding sites of Tmod1, which increased its affinity to short γ- and δ-tropomyosin isoforms, caused a decrease in binding short α-tropomyosin isoforms along with a 2-fold decrease in the length of neurites. Our data demonstrate that Tmod1 is involved in neuronal differentiation for proper neurite formation and outgrowth, and that Tmod2 inhibits these processes. The mutations in the tropomyosin-binding site of Tmod1 impair neurite outgrowth, suggesting that the integrity of this binding site is critical for the proper function of Tmod1 during neuronal differentiation.

Indexed as

ActinCytoskeletonNeurite formationTropomodulinTropomyosin

Identifiers

PMID23638401
PMCPMC3628370
OpenAlexW2028776035

What OpenQuestion holds

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LicenceCC BY
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.