Evidence map›Paper›PMID 20807799›Full record

ArticleJournal of cell science2010

The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast.

Arthur T Coulton, Daniel A East, Agnieszka Galinska-Rakoczy, William Lehman, Daniel P Mulvihill

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
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  5. InPathogens (Basel, Switzerland) · 2025
    Article
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  7. Article
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  9. Article
  10. Article
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  12. Review
  13. Article
  14. Review
  15. The Unusual Suspects in Cytokinesis: Fitting the Pieces Together.Frontiers in cell and developmental biology · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Spotlight on protein N-terminal acetylation.Experimental & molecular medicine · 2018
    Review
  20. 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

5 authors at 2 institutions in 2 countries.

Arthur T CoultonSchool of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.
Daniel A East
Agnieszka Galinska-Rakoczy
William Lehman
Daniel P Mulvihill
University of Kent · GBBoston University · US

Funding

Structure-Function of the CytoskeletonP01HL086655 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 2007 to 2011
$8.8M
THIN FILAMENTS AND VERTEBRATE SMOOTH MUSCLE CONTRACTIONR01HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI William J Lehman · 1986 to 2026
$6.5M
Thin Filaments and Muscle RegulationR37HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEHMAN, WILLIAM J · 2008 to 2017
$4.1M
THIN FILAMENTS AND VERTEBRATE SMOOTH MUSCLE CONTRACTIONR55HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEHMAN, WILLIAM J · 1992 to 1992
–
Biotechnology and Biological Sciences Research Council BB/F011784/1Biotechnology and Biological Sciences Research Council JF20605NHLBI NIH HHS HL36153NHLBI NIH HHS HL86655NHLBI NIH HHS P01 HL086655NHLBI NIH HHS R01 HL036153NHLBI NIH HHS R37 HL036153
6 · The paper itself

Abstract

Tropomyosin (Tm) is a conserved dimeric coiled-coil protein, which forms polymers that curl around actin filaments in order to regulate actomyosin function. Acetylation of the Tm N-terminal methionine strengthens end-to-end bonds, which enhances actin binding as well as the ability of Tm to regulate myosin motor activity in both muscle and non-muscle cells. In this study we explore the function of each Tm form within fission yeast cells. Electron microscopy and live cell imaging revealed that acetylated and unacetylated Tm associate with distinct actin structures within the cell, and that each form has a profound effect upon the shape and integrity of the polymeric actin filament. We show that, whereas Tm acetylation is required to regulate the in vivo motility of class II myosins, acetylated Tm had no effect on the motility of class I and V myosins. These findings illustrate a novel Tm-acetylation-state-dependent mechanism for regulating specific actomyosin cytoskeletal interactions.

Indexed as

AcetylationAcetyltransferasesActinsCell CycleCell Cycle ProteinsCytoskeletonMyosinsProtein BindingSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence DeletionTropomyosinAcetyltransferasesActinsCdc8 protein, S pombeCell Cycle ProteinsMyosinsSchizosaccharomyces pombe ProteinsTropomyosin

Identifiers

PMID20807799
PMCPMC2939800
OpenAlexW2122265029

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.