Evidence map›Paper›PMID 22483112›Full record

ArticleStructure (London, England : 1993)2012

Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling.

Paul R Elliott, Andrew F Irvine, Hyun Suk Jung, Kaeko Tozawa, Martyna W Pastok, Remigio Picone, Sandip K Badyal, Jaswir Basran, Philip S Rudland, Roger Barraclough and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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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

14 authors at 4 institutions in 2 countries.

Paul R ElliottInstitute of Integrative Biology, BioSciences Building, Crown Street, University of Liverpool, Liverpool L69 7ZB, UK.
Andrew F Irvine
Hyun Suk Jung
Kaeko Tozawa
Martyna W Pastok
Remigio Picone
Sandip K Badyal
Jaswir Basran
Philip S Rudland
Roger Barraclough
Lu-Yun Lian
Clive R Bagshaw
Marina Kriajevska
Igor L Barsukov
University of Liverpool · GBUniversity of Leicester · GBKorea Basic Science Institute · KRMRC Laboratory for Molecular Cell Biology · GB

Funding

STRUCTURE OF CONTRACTILE FILAMENTS OF MUSCLER01AR034711 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CRAIG, ROGER W · 1986 to 2013
$3.6M
Biotechnology and Biological Sciences Research Council BB/F007213/1Biotechnology and Biological Sciences Research Council BB/F00768X/1NIAMS NIH HHS R01 AR034711Wellcome Trust
6 · The paper itself

Abstract

Filament assembly of nonmuscle myosin IIA (NMIIA) is selectively regulated by the small Ca²⁺-binding protein, S100A4, which causes enhanced cell migration and metastasis in certain cancers. Our NMR structure shows that an S100A4 dimer binds to a single myosin heavy chain in an asymmetrical configuration. NMIIA in the complex forms a continuous helix that stretches across the surface of S100A4 and engages the Ca²⁺-dependent binding sites of each subunit in the dimer. Synergy between these sites leads to a very tight association (K(D) ∼1 nM) that is unique in the S100 family. Single-residue mutations that remove this synergy weaken binding and ameliorate the effects of S100A4 on NMIIA filament assembly and cell spreading in A431 human epithelial carcinoma cells. We propose a model for NMIIA filament disassembly by S100A4 in which initial binding to the unstructured NMIIA tail initiates unzipping of the coiled coil and disruption of filament packing.

Indexed as

Amino Acid SequenceBinding SitesCalciumCell Line, TumorCell MovementCytoskeletonEpithelial CellsHumansKineticsModels, MolecularMolecular Sequence DataNonmuscle Myosin Type IIANuclear Magnetic Resonance, BiomolecularPoint MutationProtein BindingProtein MultimerizationCalciumNonmuscle Myosin Type IIARecombinant ProteinsS100A4 protein, humanS100 Calcium-Binding Protein A4S100 Proteins

Identifiers

PMID22483112
PMCPMC3343272
OpenAlexW1999865803

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.