Evidence map›Paper›PMID 10512853›Full record

ArticleMolecular biology of the cell1999

Caldesmon inhibits nonmuscle cell contractility and interferes with the formation of focal adhesions.

D M Helfman, E T Levy, C Berthier, M Shtutman, D Riveline, I Grosheva, A Lachish-Zalait, M Elbaum, A D Bershadsky

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

62 citing papers in PubMed, 196 citations in OpenAlex.

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  13. Investigating cell mechanics with atomic force microscopy.Journal of the Royal Society, Interface · 2015
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2 more citing papers are in PubMed but not listed here.

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

9 authors at 3 institutions in 3 countries.

D M HelfmanCold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA.
E T Levy
C Berthier
M Shtutman
D Riveline
I Grosheva
A Lachish-Zalait
M Elbaum
A D Bershadsky
Institute of Molecular and Cell Biology · RUCold Spring Harbor Laboratory · USWeizmann Institute of Science · IL

Funding

TROPOMYOSIN IN NORMAL AND TRANSFORMED CELLSR01CA058607 · NCI · COLD SPRING HARBOR LABORATORY · PI HELFMAN, DAVID M · 1993 to 1997
–
NCI NIH HHS CA58607
6 · The paper itself

Abstract

Caldesmon is known to inhibit the ATPase activity of actomyosin in a Ca(2+)-calmodulin-regulated manner. Although a nonmuscle isoform of caldesmon is widely expressed, its functional role has not yet been elucidated. We studied the effects of nonmuscle caldesmon on cellular contractility, actin cytoskeletal organization, and the formation of focal adhesions in fibroblasts. Transient transfection of nonmuscle caldesmon prevents myosin II-dependent cell contractility and induces a decrease in the number and size of tyrosine-phosphorylated focal adhesions. Expression of caldesmon interferes with Rho A-V14-mediated formation of focal adhesions and stress fibers as well as with formation of focal adhesions induced by microtubule disruption. This inhibitory effect depends on the actin- and myosin-binding regions of caldesmon, because a truncated variant lacking both of these regions is inactive. The effects of caldesmon are blocked by the ionophore A23187, thapsigargin, and membrane depolarization, presumably because of the ability of Ca(2+)-calmodulin or Ca(2+)-S100 proteins to antagonize the inhibitory function of caldesmon on actomyosin contraction. These results indicate a role for nonmuscle caldesmon in the physiological regulation of actomyosin contractility and adhesion-dependent signaling and further demonstrate the involvement of contractility in focal adhesion formation.

Indexed as

1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineActomyosinAnimalsBotulinum ToxinsCalcimycinCalcium-Binding ProteinsCalmodulin-Binding ProteinsCell Line, TransformedCytoskeletonEnzyme InhibitorsGene ExpressionGreen Fluorescent ProteinsHumansIonophoresLuminescent ProteinsMicroscopy, Fluorescence1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineActomyosinBotulinum ToxinsCalcimycinCalcium-Binding ProteinsCalmodulin-Binding ProteinsEnzyme InhibitorsGreen Fluorescent ProteinsIonophoresLuminescent ProteinsNocodazoleThapsigargin

Identifiers

PMID10512853
PMCPMC25564
OpenAlexW2135942163

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.