Evidence map›Paper›PMID 27091317›Full record

ArticleArchives of biochemistry and biophysics2016

Tropomyosin-binding properties modulate competition between tropomodulin isoforms.

Mert Colpan, Natalia A Moroz, Kevin T Gray, Dillon A Cooper, Christian A Diaz, Alla S Kostyukova

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 19 citations in OpenAlex.

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  8. Article
  9. Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019
    Review
  10. Review
  11. Tropomodulin Isoform-Specific Regulation of Dendrite Development and Synapse Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. 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

6 authors at 1 institution in 1 country.

Mert ColpanVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States. Electronic address: mert.colpan@wsu.edu.
Natalia A MorozVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States.
Kevin T GrayVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States.
Dillon A CooperVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States.
Christian A DiazVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States.
Alla S KostyukovaVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA 99164-6515, United States. Electronic address: alla.kostyukova@wsu.edu.
Washington State University · US

Funding

TRAINING IN BIOTECHNOLOGY: EMPHASIS ON PROTEIN CHEMISTRYT32GM008336 · NIGMS · WASHINGTON STATE UNIVERSITY · PI CALL, DOUGLAS R. · 1989 to 2023
$8.9M
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 GM081688NIGMS NIH HHS T32 GM008336
6 · The paper itself

Abstract

The formation and fine-tuning of cytoskeleton in cells are governed by proteins that influence actin filament dynamics. Tropomodulin (Tmod) regulates the length of actin filaments by capping the pointed ends in a tropomyosin (TM)-dependent manner. Tmod1, Tmod2 and Tmod3 are associated with the cytoskeleton of non-muscle cells and their expression has distinct consequences on cell morphology. To understand the molecular basis of differences in the function and localization of Tmod isoforms in a cell, we compared the actin filament-binding abilities of Tmod1, Tmod2 and Tmod3 in the presence of Tpm3.1, a non-muscle TM isoform. Tmod3 displayed preferential binding to actin filaments when competing with other isoforms. Mutating the second or both TM-binding sites of Tmod3 destroyed its preferential binding. Our findings clarify how Tmod1, Tmod2 and Tmod3 compete for binding actin filaments. Different binding mechanisms and strengths of Tmod isoforms for Tpm3.1 contribute to their divergent functional capabilities.

Indexed as

Binding SitesProtein BindingProtein IsoformsStructure-Activity RelationshipTropomodulinTropomyosinProtein IsoformsTropomodulinTropomyosinActinCytoskeletonTropomodulinTropomyosin

Identifiers

PMID27091317
PMCPMC5079755
OpenAlexW2342667892

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.