Evidence map›Paper›PMID 33844684›Full record

ArticlePLoS biology2021

Molecular basis of F-actin regulation and sarcomere assembly via myotilin.

Julius Kostan, Miha Pavšič, Vid Puž, Thomas C Schwarz, Friedel Drepper, Sibylle Molt, Melissa Ann Graewert, Claudia Schreiner, Sara Sajko, Peter F M van der Ven and 7 more

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Early Cytoskeletal Remodeling Drives Hypertrophic Cardiomyopathy Pathogenesis inJournal of cardiovascular development and disease · 2025
    Article
  6. Article
  7. Review
  8. Mapping the interaction surface between CaNature communications · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. 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

17 authors at 5 institutions in 3 countries.

Julius KostanDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.ORCID 0000-0002-8347-111X
Miha PavšičDepartment of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Ljubljana, Slovenia.ORCID 0000-0002-2230-1758
Vid PužDepartment of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Ljubljana, Slovenia.
Thomas C SchwarzDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.ORCID 0000-0002-3812-9446
Friedel DrepperBiochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, Freiburg, Germany.ORCID 0000-0002-2043-5795
Sibylle MoltInstitute for Cell Biology, Department of Molecular Cell Biology, University of Bonn, Bonn, Germany.
Melissa Ann GraewertEuropean Molecular Biology Laboratory, Hamburg Unit, c/o DESY, Hamburg, Germany.ORCID 0000-0001-7547-636X
Claudia SchreinerDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
Sara SajkoDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
Peter F M van der VenInstitute for Cell Biology, Department of Molecular Cell Biology, University of Bonn, Bonn, Germany.ORCID 0000-0002-9750-8913
Adekunle OnipeDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.ORCID 0000-0001-7071-1295
Dmitri I SvergunEuropean Molecular Biology Laboratory, Hamburg Unit, c/o DESY, Hamburg, Germany.
Bettina WarscheidBiochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, Freiburg, Germany.ORCID 0000-0001-5096-1975
Robert KonratDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.
Dieter O FürstInstitute for Cell Biology, Department of Molecular Cell Biology, University of Bonn, Bonn, Germany.
Brigita LenarčičDepartment of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Ljubljana, Slovenia.ORCID 0000-0002-2508-3776
Kristina Djinović-CarugoDepartment of Structural and Computational Biology, Max Perutz Labs, University of Vienna, Vienna, Austria.ORCID 0000-0003-0252-2972
University of Vienna · ATUniversity of Bonn · DEUniversity of Ljubljana · SIEuropean Molecular Biology Laboratory · DEUniversity of Freiburg · DE

Funding

Austrian Science Fund FWF I 1593Austrian Science Fund FWF I 525Wellcome TrustWellcome Trust 201543/Z/16
6 · The paper itself

Abstract

Sarcomeres, the basic contractile units of striated muscle cells, contain arrays of thin (actin) and thick (myosin) filaments that slide past each other during contraction. The Ig-like domain-containing protein myotilin provides structural integrity to Z-discs-the boundaries between adjacent sarcomeres. Myotilin binds to Z-disc components, including F-actin and α-actinin-2, but the molecular mechanism of binding and implications of these interactions on Z-disc integrity are still elusive. To illuminate them, we used a combination of small-angle X-ray scattering, cross-linking mass spectrometry, and biochemical and molecular biophysics approaches. We discovered that myotilin displays conformational ensembles in solution. We generated a structural model of the F-actin:myotilin complex that revealed how myotilin interacts with and stabilizes F-actin via its Ig-like domains and flanking regions. Mutant myotilin designed with impaired F-actin binding showed increased dynamics in cells. Structural analyses and competition assays uncovered that myotilin displaces tropomyosin from F-actin. Our findings suggest a novel role of myotilin as a co-organizer of Z-disc assembly and advance our mechanistic understanding of myotilin's structural role in Z-discs.

Indexed as

Protein MultimerizationActin CytoskeletonActinsAnimalsCells, CulturedCytoskeletal ProteinsCytoskeletonHumansMiceMicrofilament ProteinsMuscle ContractionMuscle, SkeletalProtein BindingProtein Interaction Domains and MotifsSarcomeresTropomyosinActinsCytoskeletal ProteinsMicrofilament ProteinsMyot protein, mouseTropomyosin

Identifiers

PMID33844684
PMCPMC8062120
OpenAlexW3104597482

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.