Evidence map›Paper›PMID 15342783›Full record

ArticleMolecular biology of the cell2004

Regulation of cell motility by tyrosine phosphorylated villin.

Alok Tomar, Yaohong Wang, Narendra Kumar, Sudeep George, Bogdan Ceacareanu, Aviv Hassid, Kenneth E Chapman, Ashish M Aryal, Christopher M Waters, Seema Khurana

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 46 citations in OpenAlex.

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  7. Enterocyte loss of polarity and gut wound healing rely upon the F-actin-severing function of villin.Proceedings of the National Academy of Sciences of the United States of America · 2013
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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

10 authors at 1 institution in 1 country.

Alok TomarDepartment of Physiology, University of Tennessee Health Science Center, Memphis, TN 38163, USA.
Yaohong Wang
Narendra Kumar
Sudeep George
Bogdan Ceacareanu
Aviv Hassid
Kenneth E Chapman
Ashish M Aryal
Christopher M Waters
Seema Khurana
University of Tennessee Health Science Center · US

Funding

ROLE OF VILLIN IN EPITHELIAL CELL SIGNAL TRANSDUCTIONR01DK054755 · NIDDK · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI KHURANA, SEEMA · 2000 to 2009
$3.1M
PHYSIOLOGICAL ADAPTATION TO STRAIN IN AIRWAY EPITHELIUMR01HL064981 · NHLBI · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI WATERS, CHRISTOPHER M · 1999 to 2008
$1.9M
Regulation of epithelial cell motility by villin.R01DK065006 · NIDDK · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI KHURANA, SEEMA · 2004 to 2008
$1.6M
NHLBI NIH HHS R01 HL064981NIDDK NIH HHS DK-54755NIDDK NIH HHS DK-65006NIDDK NIH HHS R01 DK054755NIDDK NIH HHS R01 DK065006
6 · The paper itself

Abstract

Temporal and spatial regulation of the actin cytoskeleton is vital for cell migration. Here, we show that an epithelial cell actin-binding protein, villin, plays a crucial role in this process. Overexpression of villin in doxycyline-regulated HeLa cells enhanced cell migration. Villin-induced cell migration was modestly augmented by growth factors. In contrast, tyrosine phosphorylation of villin and villin-induced cell migration was significantly inhibited by the src kinase inhibitor 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP2) as well as by overexpression of a dominant negative mutant of c-src. These data suggest that phosphorylation of villin by c-src is involved in the actin cytoskeleton remodeling necessary for cell migration. We have previously shown that villin is tyrosine phosphorylated at four major sites. To further investigate the role of tyrosine phosphorylated villin in cell migration, we used phosphorylation site mutants (tyrosine to phenylalanine or tyrosine to glutamic acid) in HeLa cells. We determined that tyrosine phosphorylation at residues 60, 81, and 256 of human villin played an essential role in cell migration as well as in the reorganization of the actin cytoskeleton. Collectively, these studies define how biophysical events such as cell migration are actuated by biochemical signaling pathways involving tyrosine phosphorylation of actin binding proteins, in this case villin.

Indexed as

ActinsAdenoviridaeBinding SitesCell MovementCell ProliferationCSK Tyrosine-Protein KinaseCytoskeletonDNA, ComplementaryGenes, DominantHeLa CellsHumansMicrofilament ProteinsMicroscopy, FluorescenceMutationPhosphorylationProtein-Tyrosine KinasesActinsAG 1879CSK protein, humanCSK Tyrosine-Protein KinaseDNA, ComplementaryMicrofilament ProteinsProtein-Tyrosine KinasesPyrimidinessrc-Family KinasesTyrosinevillin

Identifiers

PMID15342783
PMCPMC524729
OpenAlexW2148287779

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.