Evidence map›Paper›PMID 27551448›Full record

ArticleCell death discovery2015

Muscle LIM protein/CSRP3: a mechanosensor with a role in autophagy.

M M Rashid, A Runci, L Polletta, I Carnevale, E Morgante, E Foglio, T Arcangeli, L Sansone, M A Russo, M Tafani

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell death discovery, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 46 citations in OpenAlex.

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  16. Generation of desminopathy in rats using CRISPR-Cas9.Journal of cachexia, sarcopenia and muscle · 2020
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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

10 authors at 2 institutions in 1 country.

M M RashidDepartment of Experimental Medicine, University of Rome , Sapienza, Rome, Italy.
A RunciDepartment of Experimental Medicine, University of Rome , Sapienza, Rome, Italy.
L PollettaDepartment of Experimental Medicine, University of Rome , Sapienza, Rome, Italy.
I CarnevaleDepartment of Experimental Medicine, University of Rome , Sapienza, Rome, Italy.
E MorganteDepartment of Experimental Medicine, University of Rome , Sapienza, Rome, Italy.
E FoglioDepartment of Experimental Medicine, University of Rome , Sapienza, Rome, Italy.
T ArcangeliDepartment of Experimental Medicine, University of Rome , Sapienza, Rome, Italy.
L SansoneDepartment of Cellular and Molecular Pathology, IRCCS San Raffaele , Rome, Italy.
M A RussoConsorzio MEBIC, San Raffaele University , Rome, Italy.
M TafaniDepartment of Experimental Medicine, University of Rome, Sapienza, Rome, Italy; Department of Cellular and Molecular Pathology, IRCCS San Raffaele, Rome, Italy.
Sapienza University of Rome · ITIRCCS Ospedale San Raffaele · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Muscle LIM protein (MLP) is a microtubule-associated protein expressed in cardiac and muscle tissues that belongs to the cysteine-rich protein (CSRP/CRP) family. MLP has a central role during muscle development and for architectural maintenance of muscle cells. However, muscle cells rely on autophagy during differentiation and for structural maintenance. To study the role of MLP in autophagy, we have used C2C12 mouse myoblasts silenced or overexpressing MLP. Our results show that MLP contributes to the correct autophagosome formation and flux by interacting with LC3 as demonstrated by co-immunoprecipitation and PLA assay. In fact, MLP silencing results in decreased LC3-II staining and absent degradation of long-lived proteins. Moreover, MLP silencing impaired myoblasts differentiation as measured by decreased expression of MyoD1, MyoG1 and myosin heavy chain. Ultrastructural analysis revealed the presence of large empty autophagosomes in myoblasts and multimembranous structures in myotubes from MLP-silenced clones. Impaired autophagy in MLP-silenced cells resulted in increased susceptibility to apoptotic cell death. In fact, treatment of MLP-silenced C2C12 myoblasts and myotubes with staurosporine resulted in increased caspase-3 and PARP cleavage as well as increased percentage of cell death. In conclusion, we propose that MLP regulates autophagy during muscle cell differentiation or maintenance through a mechanism involving MLP/LC3-II interaction and correct autophagosome formation.

Identifiers

PMID27551448
PMCPMC4981024
OpenAlexW2521702765

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.