Evidence map›Paper›PMID 20368620›Full record

ArticleThe Journal of cell biology2010

Tropomodulin isoforms regulate thin filament pointed-end capping and skeletal muscle physiology.

David S Gokhin, Raymond A Lewis, Caroline R McKeown, Roberta B Nowak, Nancy E Kim, Ryan S Littlefield, Richard L Lieber, Velia M Fowler

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.3field-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

58 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Morphological and Molecular Responses ofInternational journal of molecular sciences · 2022
    Article
  8. Article
  9. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019
    Review
  18. Review
  19. Tropomodulin Isoform-Specific Regulation of Dendrite Development and Synapse Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  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

8 authors at 2 institutions in 1 country.

David S GokhinDepartment of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Raymond A Lewis
Caroline R McKeown
Roberta B Nowak
Nancy E Kim
Ryan S Littlefield
Richard L Lieber
Velia M Fowler
Scripps Research Institute · USUniversity of California, San Diego · US

Funding

CARDIOVASCULAR SURGERY/BIOENGINEERING TRAININGT32HL007089 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHIEN, SHU · 1985 to 2009
$9.3M
Capping Actin Growth in Erythroid and Nonerythroid CellsR01HL083464 · NHLBI · UNIVERSITY OF DELAWARE · PI FOWLER, VELIA M · 2006 to 2019
$7.1M
BLOOD SYSTEMS IN COAGULATION AND VESSEL DISEASET32HL007195 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI RUF, WOLFRAM · 1985 to 2011
$5.1M
Core--ProteomicsP30EY012598 · NEI · SCRIPPS RESEARCH INSTITUTE · PI FRIEDLANDER, MARTIN · 2001 to 2005
$3.6M
Skeletal Muscle Injury: Mechanism Prevention &TreatmentR01AR040050 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LIEBER, RICHARD L · 1989 to 2007
$1.6M
Control of actin dynamics through the regulation of tropomodulinF32AR055870 · NIAMS · SCRIPPS RESEARCH INSTITUTE, THE · PI LEWIS, RAYMOND A · 2008 to 2008
$50k
NEI NIH HHS P30 EY012598NEI NIH HHS P30-EY12598NHLBI NIH HHS HL007195NHLBI NIH HHS HL083464NHLBI NIH HHS R01 HL083464NHLBI NIH HHS T32 HL007089NHLBI NIH HHS T32 HL007195NIAMS NIH HHS AR40050NIAMS NIH HHS F32 AR055870NIAMS NIH HHS R01 AR040050
6 · The paper itself

Abstract

During myofibril assembly, thin filament lengths are precisely specified to optimize skeletal muscle function. Tropomodulins (Tmods) are capping proteins that specify thin filament lengths by controlling actin dynamics at pointed ends. In this study, we use a genetic targeting approach to explore the effects of deleting Tmod1 from skeletal muscle. Myofibril assembly, skeletal muscle structure, and thin filament lengths are normal in the absence of Tmod1. Tmod4 localizes to thin filament pointed ends in Tmod1-null embryonic muscle, whereas both Tmod3 and -4 localize to pointed ends in Tmod1-null adult muscle. Substitution by Tmod3 and -4 occurs despite their weaker interactions with striated muscle tropomyosins. However, the absence of Tmod1 results in depressed isometric stress production during muscle contraction, systemic locomotor deficits, and a shift to a faster fiber type distribution. Thus, Tmod3 and -4 compensate for the absence of Tmod1 structurally but not functionally. We conclude that Tmod1 is a novel regulator of skeletal muscle physiology.

Indexed as

Actin CytoskeletonAnimalsEmbryo, MammalianMiceMice, TransgenicMuscle, SkeletalProtein IsoformsTropomodulinProtein IsoformsTmod1 protein, mouseTmod3 protein, mouseTmod4 protein, mouseTropomodulin

Identifiers

PMID20368620
PMCPMC2854367
OpenAlexW2144063416

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.