Evidence map›Paper›PMID 22016770›Full record

ArticlePloS one2011

Multi-tasking role of the mechanosensing protein Ankrd2 in the signaling network of striated muscle.

Anna Belgrano, Ljiljana Rakicevic, Lorenza Mittempergher, Stefano Campanaro, Valentina C Martinelli, Vincent Mouly, Giorgio Valle, Snezana Kojic, Georgine Faulkner

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. ANKRD1 expression and functional mechanism in stomach adenocarcinoma.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
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  12. Molecular Regulation of Exercise-Induced Muscle Fiber Hypertrophy.Cold Spring Harbor perspectives in medicine · 2018
    Review
  13. Article
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  19. Probing muscle ankyrin-repeat protein (MARP) structure and function.Anatomical record (Hoboken, N.J. : 2007) · 2014
    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

9 authors at 4 institutions in 3 countries.

Anna BelgranoMuscle Molecular Biology Group, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Ljiljana Rakicevic
Lorenza Mittempergher
Stefano Campanaro
Valentina C Martinelli
Vincent Mouly
Giorgio Valle
Snezana Kojic
Georgine Faulkner
University of Padua · ITInternational Centre for Genetic Engineering and Biotechnology · ITUniversity of Belgrade · RSSorbonne Université · FR

Funding

Telethon GGP04088Telethon GSP04289
6 · The paper itself

Abstract

backgroundAnkrd2 (also known as Arpp) together with Ankrd1/CARP and DARP are members of the MARP mechanosensing proteins that form a complex with titin (N2A)/calpain 3 protease/myopalladin. In muscle, Ankrd2 is located in the I-band of the sarcomere and moves to the nucleus of adjacent myofibers on muscle injury. In myoblasts it is predominantly in the nucleus and on differentiation shifts from the nucleus to the cytoplasm. In agreement with its role as a sensor it interacts both with sarcomeric proteins and transcription factors. METHODOLOGY/PRINCIPAL

findingsExpression profiling of endogenous Ankrd2 silenced in human myotubes was undertaken to elucidate its role as an intermediary in cell signaling pathways. Silencing Ankrd2 expression altered the expression of genes involved in both intercellular communication (cytokine-cytokine receptor interaction, endocytosis, focal adhesion, tight junction, gap junction and regulation of the actin cytoskeleton) and intracellular communication (calcium, insulin, MAPK, p53, TGF-β and Wnt signaling). The significance of Ankrd2 in cell signaling was strengthened by the fact that we were able to show for the first time that Nkx2.5 and p53 are upstream effectors of the Ankrd2 gene and that Ankrd1/CARP, another MARP member, can modulate the transcriptional ability of MyoD on the Ankrd2 promoter. Another novel finding was the interaction between Ankrd2 and proteins with PDZ and SH3 domains, further supporting its role in signaling. It is noteworthy that we demonstrated that transcription factors PAX6, LHX2, NFIL3 and MECP2, were able to bind both the Ankrd2 protein and its promoter indicating the presence of a regulatory feedback loop mechanism. CONCLUSIONS/SIGNIFICANCE: In conclusion we demonstrate that Ankrd2 is a potent regulator in muscle cells affecting a multitude of pathways and processes.

Indexed as

Mechanotransduction, CellularAnimalsCell LineHomeobox Protein Nkx-2.5Homeodomain ProteinsHumansMuscle Fibers, SkeletalMuscle ProteinsMuscle, StriatedMyoD ProteinNuclear ProteinsPDZ DomainsPromoter Regions, GeneticRepressor ProteinsRNA Interferencesrc Homology DomainsANKRD1 protein, humanANKRD2 protein, humanHomeobox Protein Nkx-2.5Homeodomain ProteinsMuscle ProteinsMyoD ProteinNKX2-5 protein, humanNuclear ProteinsRepressor ProteinsTranscription FactorsTumor Suppressor Protein p53

Identifiers

PMID22016770
PMCPMC3189947
OpenAlexW2000817502

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.