Evidence map›Paper›PMID 33077830›Full record

ArticleScientific reports2020

Cytoskeletal disorganization underlies PABPN1-mediated myogenic disability.

Cyriel Sebastiaan Olie, Erik van der Wal, Domagoj Cikes, Loes Maton, Jessica C de Greef, I-Hsuan Lin, Yi-Fan Chen, Elsayad Kareem, Josef M Penninger, Benedikt M Kessler and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

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  6. Brillouin microscopy.Nature reviews. Methods primers · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 7 institutions in 4 countries.

Cyriel Sebastiaan OlieHuman Genetics Department, Leiden University Medical Center, Leiden, The Netherlands.
Erik van der WalHuman Genetics Department, Leiden University Medical Center, Leiden, The Netherlands.
Domagoj CikesIMBA-Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.
Loes MatonHuman Genetics Department, Leiden University Medical Center, Leiden, The Netherlands.
Jessica C de GreefHuman Genetics Department, Leiden University Medical Center, Leiden, The Netherlands.
I-Hsuan LinVYM Genome Research Center, National Yang-Ming University, Taipei, Taiwan.
Yi-Fan ChenCollege of Medical Science and Technology, Taipei Medical University, Taipei, Taiwan.
Elsayad KareemAdvanced Microscopy Facility, Vienna Biocenter Core Facilities, Vienna Biocenter (VBC), Vienna, Austria.
Josef M PenningerIMBA-Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.
Benedikt M KesslerTarget Discovery Institute, Nuffield, Department of Medicine, University of Oxford, Oxford, UK.
Vered RazHuman Genetics Department, Leiden University Medical Center, Leiden, The Netherlands. V.Raz@lumc.nl.
Leiden University Medical Center · NLAustrian Academy of Sciences · ATInstitute of Molecular Biotechnology · ATNational Yang Ming Chiao Tung University · TWTaipei Medical University · TWUniversity of Oxford · GBVienna Biocenter · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Muscle wasting and atrophy are regulated by multiple molecular processes, including mRNA processing. Reduced levels of the polyadenylation binding protein nucleus 1 (PABPN1), a multifactorial regulator of mRNA processing, cause muscle atrophy. A proteomic study in muscles with reduced PABPN1 levels suggested dysregulation of sarcomeric and cytoskeletal proteins. Here we investigated the hypothesis that reduced PABPN1 levels lead to an aberrant organization of the cytoskeleton. MURC, a plasma membrane-associated protein, was found to be more abundant in muscles with reduced PABPN1 levels, and it was found to be expressed at regions showing regeneration. A polarized cytoskeletal organization is typical for muscle cells, but muscle cells with reduced PABPN1 levels (named as shPAB) were characterized by a disorganized cytoskeleton that lacked polarization. Moreover, cell mechanical features and myogenic differentiation were significantly reduced in shPAB cells. Importantly, restoring cytoskeletal stability, by actin overexpression, was beneficial for myogenesis, expression of sarcomeric proteins and proper localization of MURC in shPAB cell cultures and in shPAB muscle bundle. We suggest that poor cytoskeletal mechanical features are caused by altered expression levels of cytoskeletal proteins and contribute to muscle wasting and atrophy.

Indexed as

ActinsCell LineCytoskeletonHumansMuscle DevelopmentMuscle, SkeletalMuscular AtrophyPoly(A)-Binding Protein IActinsPABPN1 protein, humanPoly(A)-Binding Protein I

Identifiers

PMID33077830
PMCPMC7572364
OpenAlexW3092725575

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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.