Evidence map›Paper›PMID 24647531›Full record

ArticlePloS one2014

ZASP interacts with the mechanosensing protein Ankrd2 and p53 in the signalling network of striated muscle.

Valentina C Martinelli, W Buck Kyle, Snezana Kojic, Nicola Vitulo, Zhaohui Li, Anna Belgrano, Paolo Maiuri, Lawrence Banks, Matteo Vatta, Giorgio Valle and 1 more

RetractedOpen access · goldAbstract readRetracted Publication
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022
    Review
  6. The unexpected versatility of ALP/Enigma family proteins.Frontiers in cell and developmental biology · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. The Role of Z-disc Proteins in Myopathy and Cardiomyopathy.International journal of molecular sciences · 2021
    Review
  11. Panorama of the distal myopathies.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2020
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Inherited cardiomyopathies.Circulation journal : official journal of the Japanese Circulation Society · 2014
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 4 countries.

Valentina C MartinelliInternational Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
W Buck KyleDepartment of Paediatrics (Cardiology), Baylor College of Medicine, Houston, Texas, United States of America.
Snezana KojicLaboratory of Molecular Biology, Institute of Molecular Genetics and Genetic Engineering, University of Belgrade, Belgrade, Serbia.
Nicola VituloCentro di Ricerca Interdipartimentale per le Biotecnologie Innovative, University of Padua, Padova, Italy.
Zhaohui LiDepartment of Paediatrics (Cardiology), Baylor College of Medicine, Houston, Texas, United States of America.
Anna BelgranoInternational Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Paolo MaiuriInternational Centre for Genetic Engineering and Biotechnology, Trieste, Italy; Systems Cell Biology of Cell Polarity and Cell Division, Institut Curie, Paris, France.
Lawrence BanksInternational Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Matteo VattaDepartment of Paediatrics (Cardiology), Baylor College of Medicine, Houston, Texas, United States of America; Department of Medical and Molecular Genetics, University of Indiana, Indianapolis, Indiana, United States of America.
Giorgio ValleCentro di Ricerca Interdipartimentale per le Biotecnologie Innovative, University of Padua, Padova, Italy.
Georgine FaulknerInternational Centre for Genetic Engineering and Biotechnology, Trieste, Italy; Centro di Ricerca Interdipartimentale per le Biotecnologie Innovative, University of Padua, Padova, Italy.
International Centre for Genetic Engineering and Biotechnology · ITBaylor College of Medicine · USUniversity of Padua · ITInstitut Curie · FRUniversity of Belgrade · RS

Funding

HEART-LUNG PHYSIOLOGY: MOLECULAR-SYSTEMIC INTEGRATIONT32HL007887 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI SCHILLING, WILLIAM P · 1999 to 2008
$2.5M
NHLBI NIH HHS R21-HL07887NHLBI NIH HHS T32 HL007887
6 · The paper itself

Abstract

ZASP is a cytoskeletal PDZ-LIM protein predominantly expressed in striated muscle. It forms multiprotein complexes and plays a pivotal role in the structural integrity of sarcomeres. Mutations in the ZASP protein are associated with myofibrillar myopathy, left ventricular non-compaction and dilated cardiomyopathy. The ablation of its murine homologue Cypher results in neonatal lethality. ZASP has several alternatively spliced isoforms, in this paper we clarify the nomenclature of its human isoforms as well as their dynamics and expression pattern in striated muscle. Interaction is demonstrated between ZASP and two new binding partners both of which have roles in signalling, regulation of gene expression and muscle differentiation; the mechanosensing protein Ankrd2 and the tumour suppressor protein p53. These proteins and ZASP form a triple complex that appears to facilitate poly-SUMOylation of p53. We also show the importance of two of its functional domains, the ZM-motif and the PDZ domain. The PDZ domain can bind directly to both Ankrd2 and p53 indicating that there is no competition between it and p53 for the same binding site on Ankrd2. However there is competition for this binding site between p53 and a region of the ZASP protein lacking the PDZ domain, but containing the ZM-motif. ZASP is negative regulator of p53 in transactivation experiments with the p53-responsive promoters, MDM2 and BAX. Mutations in the ZASP ZM-motif induce modification in protein turnover. In fact, two mutants, A165V and A171T, were not able to bind Ankrd2 and bound only poorly to alpha-actinin2. This is important since the A165V mutation is responsible for zaspopathy, a well characterized autosomal dominant distal myopathy. Although the mechanism by which this mutant causes disease is still unknown, this is the first indication of how a ZASP disease associated mutant protein differs from that of the wild type ZASP protein.

Indexed as

Signal TransductionActininAdaptor Proteins, Signal TransducingAnimalsAnkyrin Repeatbcl-2-Associated X ProteinBinding SitesCell LineFluorescence Recovery After PhotobleachingHumansIntracellular SpaceLIM Domain ProteinsMiceMuscle ProteinsMuscle, StriatedMutant ProteinsActininACTN2 protein, humanAdaptor Proteins, Signal TransducingANKRD2 protein, humanbcl-2-Associated X ProteinLDB3 protein, humanLIM Domain ProteinsMDM2 protein, humanMuscle ProteinsMutant ProteinsNuclear ProteinsProtein IsoformsProto-Oncogene Proteins c-mdm2Repressor ProteinsTumor Suppressor Protein p53

Identifiers

PMID24647531
PMCPMC3960238
OpenAlexW1964117666

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.