Evidence map›Paper›PMID 19553683›Full record

ArticleThe Journal of biological chemistry2009

Myosin II tailpiece determines its paracrystal structure, filament assembly properties, and cellular localization.

Daniel Ronen, Shoshana Ravid

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024
    Review
  4. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Mammalian nonmuscle myosin II comes in three flavors.Biochemical and biophysical research communications · 2018
    Review
  12. Article
  13. Ordering of myosin II filaments driven by mechanical forces: experiments and theory.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
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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

2 authors.

Daniel RonenDepartment of Biochemistry and Molecular Biology, the Institute for Medical Research, Israel-Canada, the Hebrew University, Hadassah Medical School, Jerusalem 91220, Israel.
Shoshana Ravid

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Non muscle myosin II (NMII) is a major motor protein present in all cell types. The three known vertebrate NMII isoforms share high sequence homology but play different cellular roles. The main difference in sequence resides in the C-terminal non-helical tailpiece (tailpiece). In this study we demonstrate that the tailpiece is crucial for proper filament size, overcoming the intrinsic properties of the coiled-coil rod. Furthermore, we show that the tailpiece by itself determines the NMII filament structure in an isoform-specific manner, thus providing a possible mechanism by which each NMII isoform carries out its unique cellular functions. We further show that the tailpiece determines the cellular localization of NMII-A and NMII-B and is important for NMII-C role in focal adhesion complexes. We mapped NMII-C sites phosphorylated by protein kinase C and casein kinase II and showed that these phosphorylations affect its solubility properties and cellular localization. Thus phosphorylation fine-tunes the tailpiece effects on the coiled-coil rod, enabling dynamic regulation of NMII-C assembly. We thus show that the small tailpiece of NMII is a distinct domain playing a role in isoform-specific filament assembly and cellular functions.

Indexed as

AnimalsCasein Kinase IICell Line, TumorCrystallography, X-RayFibroblastsHumansMiceMicroscopy, ElectronMyosin Type IIPhosphorylationProtein IsoformsProtein Kinase CProtein Structure, TertiaryRNA, Small InterferingWound HealingCasein Kinase IIMyosin Type IIProtein IsoformsProtein Kinase CRNA, Small Interfering

Identifiers

PMID19553683
PMCPMC2757198
OpenAlexW2029136506

What OpenQuestion holds

Textmetadata
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.