Evidence map›Paper›PMID 23727244›Full record

ArticleCell reports2013

Structural basis of actin filament nucleation by tandem W domains.

Xiaorui Chen, Fengyun Ni, Xia Tian, Elena Kondrashkina, Qinghua Wang, Jianpeng Ma

Abstract read
In one paragraph

Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Building the brush border, one microvillus at a time.Current opinion in cell biology · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Regulation of MRTF-A by JMY via a nucleation-independent mechanism.Cell communication and signaling : CCS · 2018
    Article
  11. Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. WASP family proteins, more than Arp2/3 activators.Biochemical Society transactions · 2016
    Review
  14. Article
  15. Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. 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

6 authors.

Xiaorui ChenGraduate Program of Structural and Computational Biology and Molecular Biophysics, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Fengyun Ni
Xia Tian
Elena Kondrashkina
Qinghua Wang
Jianpeng Ma

Funding

New Simulation Methods at Multi-Scales and -ResolutionsR01GM067801 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI MA, JIANPENG · 2003 to 2015
$3.4M
Structural and Functional Study of Influenza Virus HemagglutininR01AI067839 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI WANG, QINGHUA · 2009 to 2013
$1.5M
NIAID NIH HHS R01 AI067839NIAID NIH HHS R01-AI067839NIGMS NIH HHS R01 GM067801NIGMS NIH HHS R01-GM067801
6 · The paper itself

Abstract

Spontaneous nucleation of actin is very inefficient in cells. To overcome this barrier, cells have evolved a set of actin filament nucleators to promote rapid nucleation and polymerization in response to specific stimuli. However, the molecular mechanism of actin nucleation remains poorly understood. This is hindered largely by the fact that actin nucleus, once formed, rapidly polymerizes into filament, thus making it impossible to capture stable multisubunit actin nucleus. Here, we report an effective double-mutant strategy to stabilize actin nucleus by preventing further polymerization. Employing this strategy, we solved the crystal structure of AMPPNP-actin in complex with the first two tandem W domains of Cordon-bleu (Cobl), a potent actin filament nucleator. Further sequence comparison and functional studies suggest that the nucleation mechanism of Cobl is probably shared by the p53 cofactor JMY, but not Spire. Moreover, the double-mutant strategy opens the way for atomic mechanistic study of actin nucleation and polymerization.

Indexed as

Actin CytoskeletonActinsAmino Acid SequenceAnimalsCrystallography, X-RayDrosophilaHumansModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, QuaternaryProtein Structure, TertiaryActins

Identifiers

PMID23727244
PMCPMC3780403

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.