Evidence map›Paper›PMID 19736312›Full record

ArticleThe Journal of biological chemistry2009

Vinculin nucleates actin polymerization and modifies actin filament structure.

Kuo-Kuang Wen, Peter A Rubenstein, Kris A DeMali

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 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.8field-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

46 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
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  8. Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022
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  11. Transgelin-2: A Double-Edged Sword in Immunity and Cancer Metastasis.Frontiers in cell and developmental biology · 2021
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  15. Review
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  18. Mechanosensing and Mechanotransduction at Cell-Cell Junctions.Cold Spring Harbor perspectives in biology · 2018
    Review
  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 at 1 institution in 1 country.

Kuo-Kuang WenDepartment of Biochemistry, University of Iowa, Roy J and Lucille A Carver College of Medicine, Iowa City, Iowa 52242, USA.
Peter A Rubenstein
Kris A DeMali
University of Iowa · US

Funding

MUTAGENIC STUDY OF YEAST ACTIN CONFORMATIONAL CHANGESR01GM033689 · NIGMS · UNIVERSITY OF IOWA · PI RUBENSTEIN, PETER A. · 1985 to 2010
$3.7M
Role of Vinculin in Epithelial Cell JunctionsK01CA111818 · NCI · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI DEMALI, KRIS A · 2005 to 2009
$724k
NCI NIH HHS 1K01CA111818NCI NIH HHS K01 CA111818NIGMS NIH HHS GM33689NIGMS NIH HHS R01 GM033689
6 · The paper itself

Abstract

Vinculin links integrins to the actin cytoskeleton by binding F-actin. Little is known with respect to how this interaction occurs or affects actin dynamics. Here we assess the consequence of the vinculin tail (VT) on actin dynamics by examining its binding to monomeric and filamentous yeast actins. VT causes pyrene-labeled G-actin to polymerize in low ionic strength buffer (G-buffer), conditions that normally do not promote actin polymerization. Analysis by electron microscopy shows that, under these conditions, the filaments form small bundles at low VT concentrations, which gradually increase in size until saturation occurs at a ratio of 2 VT:1 actin. Addition of VT to pyrene-labeled mutant yeast G-actin (S265C) produced a fluorescence excimer band, which requires a relatively normal filament geometry. In higher ionic strength polymerization-promoting F-buffer, substoichiometric amounts of VT accelerate the polymerization of pyrene-labeled WT actin. However, the amplitude of the pyrene fluorescence caused by actin polymerization is quenched as the VT concentration increases without an effect on net actin polymerization as determined by centrifugation assays. Finally, addition of VT to preformed pyrene-labeled S265C F-actin causes a concentration-dependent decrease in the maximum amplitude of the pyrene fluorescence band demonstrating the ability of VT to remodel the conformation of the actin filament. These observations support the idea that vinculin can link adhesion plaques to the cytoskeleton by initiating the formation of bundled actin filaments or by remodeling existing filaments.

Indexed as

Actin CytoskeletonActinsAnimalsChickensCrystallizationCytoskeletonEscherichia coliMicroscopy, ElectronProtein BindingProtein ConformationVinculinYeastsActinsVinculin

Identifiers

PMID19736312
PMCPMC2781601
OpenAlexW1979660397

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.