Evidence map›Paper›PMID 12631719›Full record

ArticleMolecular biology of the cell2003

Specification of actin filament function and molecular composition by tropomyosin isoforms.

Nicole S Bryce, Galina Schevzov, Vicki Ferguson, Justin M Percival, Jim J-C Lin, Fumio Matsumura, James R Bamburg, Peter L Jeffrey, Edna C Hardeman, Peter Gunning and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

112 citing papers in PubMed, 248 citations in OpenAlex.

  1. Review
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  12. Review
  13. Research Advances in the Role of the Tropomyosin Family in Cancer.International journal of molecular sciences · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Synaptic tau: A pathological or physiological phenomenon?Acta neuropathologica communications · 2021
    Review
  19. Article
  20. Article

52 more citing papers are in PubMed but not listed here.

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

11 authors at 7 institutions in 3 countries.

Nicole S BryceOncology Research Unit, Department of Paediatrics and Child Health, University of Sydney, The Children's Hospital at Westmead, Australia.
Galina Schevzov
Vicki Ferguson
Justin M Percival
Jim J-C Lin
Fumio Matsumura
James R Bamburg
Peter L Jeffrey
Edna C Hardeman
Peter Gunning
Ron P Weinberger
Children's Hospital at Westmead · AUUniversity of Sydney · AUChildren's Medical Research Institute · AUColorado State University · USInstitute of Developmental Physiology · RURutgers, The State University of New Jersey · USUniversity of Iowa · US

Funding

STRUCTURE/FUNCTION OF ACTIN DEPOLYMERIZING FACTORR01GM035126 · NIGMS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI BAMBURG, JAMES R · 1985 to 2003
$1.1M
NIGMS NIH HHS GM35126NIGMS NIH HHS R01 GM035126
6 · The paper itself

Abstract

The specific functions of greater than 40 vertebrate nonmuscle tropomyosins (Tms) are poorly understood. In this article we have tested the ability of two Tm isoforms, TmBr3 and the human homologue of Tm5 (hTM5(NM1)), to regulate actin filament function. We found that these Tms can differentially alter actin filament organization, cell size, and shape. hTm5(NM1) was able to recruit myosin II into stress fibers, which resulted in decreased lamellipodia and cellular migration. In contrast, TmBr3 transfection induced lamellipodial formation, increased cellular migration, and reduced stress fibers. Based on coimmunoprecipitation and colocalization studies, TmBr3 appeared to be associated with actin-depolymerizing factor/cofilin (ADF)-bound actin filaments. Additionally, the Tms can specifically regulate the incorporation of other Tms into actin filaments, suggesting that selective dimerization may also be involved in the control of actin filament organization. We conclude that Tm isoforms can be used to specify the functional properties and molecular composition of actin filaments and that spatial segregation of isoforms may lead to localized specialization of actin filament function.

Indexed as

ActinsAnimalsCell LineCell MovementCell SizeHumansMiceMice, TransgenicMyosin Type IINeuronsProtein IsoformsPseudopodiaRatsStress FibersTropomyosinActinsMyosin Type IIProtein IsoformsTPM3 protein, humanTpm3 protein, mouseTpm3 protein, ratTropomyosin

Identifiers

PMID12631719
PMCPMC151575
OpenAlexW2149966352

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.