Evidence map›Paper›PMID 27126680›Full record

ArticleCytoskeleton (Hoboken, N.J.)2016

Tropomodulin isoforms utilize specific binding functions to modulate dendrite development.

Kevin T Gray, Alexandra K Suchowerska, Tyler Bland, Mert Colpan, Gary Wayman, Thomas Fath, Alla S Kostyukova

Abstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2016. 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
1.5field-weighted citation impact, top 20% 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, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structural insights into the tropomodulin assembly at the pointed ends of actin filaments.Protein science : a publication of the Protein Society · 2021
    Article
  9. Article
  10. Tropomodulin Isoform-Specific Regulation of Dendrite Development and Synapse Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  11. Article
  12. Article
  13. Review
  14. Journal of psychiatry & neuroscience : JPN · 2017
    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

7 authors at 2 institutions in 2 countries.

Kevin T GrayVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, Washington.
Alexandra K SuchowerskaSchool of Medical Sciences, University of New South Wales, Sydney, New South Wales, Australia.
Tyler BlandDepartment of Integrative Physiology and Neuroscience, Washington State University, Pullman, Washington.
Mert ColpanVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, Washington.
Gary WaymanDepartment of Integrative Physiology and Neuroscience, Washington State University, Pullman, Washington.
Thomas FathSchool of Medical Sciences, University of New South Wales, Sydney, New South Wales, Australia.
Alla S KostyukovaVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, Washington.
Washington State University · USUNSW Sydney · AU

Funding

TRAINING IN BIOTECHNOLOGY: EMPHASIS ON PROTEIN CHEMISTRYT32GM008336 · NIGMS · WASHINGTON STATE UNIVERSITY · PI CALL, DOUGLAS R. · 1989 to 2023
$8.9M
Control of Dendritic and Synaptic Development by Extracellular CuesR01MH086032 · NIMH · WASHINGTON STATE UNIVERSITY · PI WAYMAN, GARY ALLEN · 2010 to 2014
$1.8M
NIGMS NIH HHS T32 GM008336NIMH NIH HHS R01 MH086032
6 · The paper itself

Abstract

Tropomodulins (Tmods) cap F-actin pointed ends and have altered expression in the brain in neurological diseases. The function of Tmods in neurons has been poorly studied and their role in neurological diseases is entirely unknown. In this article, we show that Tmod1 and Tmod2, but not Tmod3, are positive regulators of dendritic complexity and dendritic spine morphology. Tmod1 increases dendritic branching distal from the cell body and the number of filopodia/thin spines. Tmod2 increases dendritic branching proximal to the cell body and the number of mature dendritic spines. Tmods utilize two actin-binding sites and two tropomyosin (Tpm)-binding sites to cap F-actin. Overexpression of Tmods with disrupted Tpm-binding sites indicates that Tmod1 and Tmod2 differentially utilize their Tpm- and actin-binding sites to affect morphology. Disruption of Tmod1's Tpm-binding sites abolished the overexpression phenotype. In contrast, overexpression of the mutated Tmod2 caused the same phenotype as wild type overexpression. Proximity ligation assays indicate that the mutated Tmods are shuttled similarly to wild type Tmods. Our data begins to uncover the roles of Tmods in neural development and the mechanism by which Tmods alter neural morphology. These observations in combination with altered Tmod expression found in several neurological diseases also suggest that dysregulation of Tmod expression may be involved in the pathology of these diseases. © 2016 Wiley Periodicals, Inc.

Indexed as

AnimalsDendritesMutationPC12 CellsProtein IsoformsRatsTropomodulinProtein IsoformsTmod1 protein, ratTmod2 protein, ratTmod3 protein, ratTropomodulindendritehippocampal neuronspinetropomodulintropomyosin

Identifiers

PMID27126680
PMCPMC4916160
OpenAlexW2344098967

What OpenQuestion holds

Textmetadata
LicenceTDM
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.