Evidence map›Paper›PMID 21078954›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments.

Derek Ricketson, Christopher A Johnston, Kenneth E Prehoda

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Review
  4. Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  8. Article
  9. Article
  10. Targeting cytoskeletal phosphorylation in cancer.Exploration of targeted anti-tumor therapy · 2021
    Review
  11. TheMolecular biology of the cell · 2020
    Article
  12. Article
  13. Review
  14. Review
  15. 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
  16. Article
  17. Review
  18. Article
  19. 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

3 authors.

Derek RicketsonDepartment of Chemistry, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.
Christopher A Johnston
Kenneth E Prehoda

Funding

MOLECULAR BIOLOGY AND BIOPHYSICST32GM007759 · NIGMS · UNIVERSITY OF OREGON · PI NOLEN, BRADLEY J · 1985 to 2021
$8.5M
Protein Interactions That Regulate Cell PolarityR01GM068032 · NIGMS · UNIVERSITY OF OREGON · PI PREHODA, KENNETH E · 2003 to 2016
$4.1M
NIGMS NIH HHS GM068032NIGMS NIH HHS R01 GM068032NIGMS NIH HHS T32 GM007759
6 · The paper itself

Abstract

Contractile force transduction by myosin II derives from its assembly into bipolar filaments. The coiled-coil tail domain of the myosin II heavy chain mediates filament assembly, although the mechanism is poorly understood. Tail domains contain an alternating electrostatic repeat, yet only a small region of the tail (termed the "assembly domain") is typically required for assembly. Using computational analysis, mutagenesis, and electron microscopy we discovered that the assembly domain does not function through self-interaction as previously thought. Rather, the assembly domain acts as a unique, positively charged interaction surface that can stably contact multiple complementary, negatively charged surfaces in the upstream tail domain. The relative affinities of the assembly domain to each complementary interaction surface sets the characteristic molecular staggers observed in myosin II filaments. Together these results explain the relationship between the charge repeat and assembly domain in stabilizing myosin bipolar filaments.

Indexed as

Static ElectricityAnimalsComputer SimulationDrosophilaMicroscopy, ElectronMutagenesisMyosin Heavy ChainsMyosin Type IIProtein ConformationProtein StabilityMyosin Heavy ChainsMyosin Type II

Identifiers

PMID21078954
PMCPMC3000310

What OpenQuestion holds

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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.