Evidence map›Paper›PMID 23027950›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness.

Hyeran Kang, Michael J Bradley, Brannon R McCullough, Anaëlle Pierre, Elena E Grintsevich, Emil Reisler, Enrique M De La Cruz

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

50 citing papers in PubMed, 106 citations in OpenAlex.

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  9. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  10. Article
  11. Review
  12. Article
  13. Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  15. 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

7 authors at 3 institutions in 2 countries.

Hyeran KangDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA.
Michael J Bradley
Brannon R McCullough
Anaëlle Pierre
Elena E Grintsevich
Emil Reisler
Enrique M De La Cruz
Yale University · USUniversity of California, Los Angeles · USÉcole Normale Supérieure Paris-Saclay · FR

Funding

Dynamic Events in Myosin and Actin and Their FunctionR01GM077190 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REISLER, EMIL · 2006 to 2020
$6.2M
Actin filament elasticity and actin-binding protein functionR01GM097348 · NIGMS · YALE UNIVERSITY · PI DE LA CRUZ, ENRIQUE M · 2011 to 2018
$3.1M
NIGMS NIH HHS R01 GM077190NIGMS NIH HHS R01-GM077190NIGMS NIH HHS R01 GM097348NIGMS NIH HHS R01-GM097348
6 · The paper itself

Abstract

The assembly of actin monomers into filaments and networks plays vital roles throughout eukaryotic biology, including intracellular transport, cell motility, cell division, determining cellular shape, and providing cells with mechanical strength. The regulation of actin assembly and modulation of filament mechanical properties are critical for proper actin function. It is well established that physiological salt concentrations promote actin assembly and alter the overall bending mechanics of assembled filaments and networks. However, the molecular origins of these salt-dependent effects, particularly if they involve nonspecific ionic strength effects or specific ion-binding interactions, are unknown. Here, we demonstrate that specific cation binding at two discrete sites situated between adjacent subunits along the long-pitch helix drive actin polymerization and determine the filament bending rigidity. We classify the two sites as "polymerization" and "stiffness" sites based on the effects that mutations at the sites have on salt-dependent filament assembly and bending mechanics, respectively. These results establish the existence and location of the cation-binding sites that confer salt dependence to the assembly and mechanics of actin filaments.

Indexed as

Models, MolecularPolymerizationActinsAmino AcidsAnimalsBiomechanical PhenomenaCationsComputational BiologyFluorescenceRabbitsThermodynamicsActinsAmino AcidsCations

Identifiers

PMID23027950
PMCPMC3479481
OpenAlexW2063534876

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.