Evidence map›Paper›PMID 24798732›Full record

ArticleThe Journal of cell biology2014

Actin scaffolding by clathrin heavy chain is required for skeletal muscle sarcomere organization.

Stéphane Vassilopoulos, Christel Gentil, Jeanne Lainé, Pierre-Olivier Buclez, Agathe Franck, Arnaud Ferry, Guillaume Précigout, Robyn Roth, John E Heuser, Frances M Brodsky and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

36 citing papers in PubMed, 71 citations in OpenAlex.

  1. Relaxin-2: Shaping the Proteomic Landscape of Skeletal Muscle Physiology, Glucose Trafficking, and Mitochondrial Function in Rat.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
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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

15 authors at 7 institutions in 3 countries.

Stéphane VassilopoulosInstitut National de la Santé et de la Recherche Médicale (INSERM) U974, 2 Centre National de la Recherche Scientifique (CNRS) UMR 7215, and 3 Université Pierre et Marie Curie-Paris 6, UM 76, Paris F-75013, France.
Christel Gentil
Jeanne Lainé
Pierre-Olivier Buclez
Agathe Franck
Arnaud Ferry
Guillaume Précigout
Robyn Roth
John E Heuser
Frances M Brodsky
Luis Garcia
Gisèle Bonne
Thomas Voit
France Piétri-Rouxel
Marc Bitoun
Institut de Myologie · FRInserm · FRSorbonne Université · FRWashington University in St. Louis · USCentre National de la Recherche Scientifique · FRCentre National pour la Recherche Scientifique et Technique (CNRST) · MAUniversity of California, San Francisco · US

Funding

THE MOLECULAR MECHANISM OF CLATHRIN ASSEMBLYR01GM038093 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BRODSKY, FRANCES M. · 1988 to 2014
$5.0M
NIGMS NIH HHS GM038093NIGMS NIH HHS R01 GM038093
6 · The paper itself

Abstract

The ubiquitous clathrin heavy chain (CHC), the main component of clathrin-coated vesicles, is well characterized for its role in intracellular membrane traffic and endocytosis from the plasma membrane (PM). Here, we demonstrate that in skeletal muscle CHC regulates the formation and maintenance of PM-sarcomere attachment sites also known as costameres. We show that clathrin forms large coated lattices associated with actin filaments and the muscle-specific isoform of α-actinin at the PM of differentiated myotubes. Depletion of CHC in myotubes induced a loss of actin and α-actinin sarcomeric organization, whereas CHC depletion in vivo induced a loss of contractile force due to the detachment of sarcomeres from the PM. Our results suggest that CHC contributes to the formation and maintenance of the contractile apparatus through interactions with costameric proteins and highlight an unconventional role for CHC in skeletal muscle that may be relevant to pathophysiology of neuromuscular disorders.

Indexed as

3T3 CellsActin CytoskeletonActininActinsAdaptor Proteins, Signal TransducingAnimalsClathrin Heavy ChainsCostameresDependovirusDNA-Binding ProteinsDynamin IIGenetic VectorsGene Transfer TechniquesMiceMice, Inbred C57BLMicrofilament ProteinsActininActinsAdaptor Proteins, Signal TransducingClathrin Heavy ChainsDNA-Binding ProteinsDynamin IIHip1r protein, mouseMicrofilament Proteins

Identifiers

PMID24798732
PMCPMC4018784
OpenAlexW2047623759

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.