Evidence map›Paper›PMID 17381546›Full record

ArticleDifferentiation; research in biological diversity2007

Differentiation of cardiomyocytes requires functional serine residues within the amino-terminal domain of desmin.

Alexandra Höllrigl, Manuela Hofner, Martina Stary, Georg Weitzer

Open access · greenAbstract read
In one paragraph

Article in Differentiation; research in biological diversity, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. A cytoplasmic escapee: desmin is going nuclear.Turkish journal of biology = Turk biyoloji dergisi · 2021
    Review
  4. Review
  5. Review
  6. Article
  7. Autophagic vacuolar pathology in desminopathies.Neuromuscular disorders : NMD · 2015
    Article
  8. Desmin related disease: a matter of cell survival failure.Current opinion in cell biology · 2015
    Review
  9. Phosphorylation of tropomodulin1 contributes to the regulation of actin filament architecture in cardiac muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014
    Article
  10. Μyospryn: a multifunctional desmin-associated protein.Histochemistry and cell biology · 2013
    Review
  11. Mechanisms of cardiogenesis in cardiovascular progenitor cells.International review of cell and molecular biology · 2012
    Review
  12. Article
  13. Review
  14. 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

4 authors at 2 institutions in 2 countries.

Alexandra HöllriglMax F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Dr. Bohrgasse 9, A1030 Vienna, Austria.
Manuela Hofner
Martina Stary
Georg Weitzer
In-Q-Tel · USMedical University of Vienna · AT

Funding

Austrian Science Fund FWF P 18659
6 · The paper itself

Abstract

Desmin contributes to the stability of the myocardium and its amino-terminal domain influences intermediate filament formation and interacts with a variety of proteins and DNAs. Specific serine residues located in this domain are reversibly phosphorylated in a cell cycle and developmental stage-dependent manner as has been demonstrated also for other cytoplasmic type III intermediate filament proteins. Although absence of desmin apparently does not affect cardiomyogenesis, homozygous deletion of the amino-terminal domain of desmin severely inhibited in vitro cardiomyogenesis. To demonstrate the significance of phosphorylation of this domain in cardiomyogenic commitment and differentiation, we inhibited phosphorylation of serine residues 6, 7, and 8 by mutation to alanine, and investigated early cardiomyogenesis in heterozygous embryoid bodies. As control, serine residues 31 and 32, which are not phosphorylated by kinases mutating serine residues 6, 7, and 8, were mutated to alanine in a second set. Desmin(S6,7,8A) interfered with cardiomyogenesis and myofibrillogenesis in a dominant negative fashion, whereas desmin(S31,32A) produced only a mild phenotype. Desmin(S6,7,8A) led to the down-regulation of the transcription factor genes brachyury, goosecoid, nkx2.5, and mef2C and increased apoptosis of presumptive mesoderm and differentiating cardiomyocytes. Surviving cardiomyocytes which were few in number had no myofibrils. Demonstration that some but not any mutant desmin interfered with the very beginning of cardiomyogenesis suggests an important function of temporarily phosphorylated serine residues 6, 7, and 8 in the amino-terminal domain of desmin in cardiomyogenic commitment and differentiation.

Indexed as

AnimalsCell DifferentiationCell LineCell ProliferationDesminHumansMuscle DevelopmentMyocytes, CardiacPeptide FragmentsProtein Structure, TertiarySerineTranscription FactorsDesminPeptide FragmentsSerineTranscription Factors

Identifiers

PMID17381546
PMCPMC7615843
OpenAlexW2073224928

What OpenQuestion holds

Textmetadata
LicenceTDM
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.