Evidence map›Paper›PMID 12783627›Full record

ArticleBMC cell biology2003

Rapid de-localization of actin leading edge components with BDM treatment.

Justin C Yarrow, Terry Lechler, Rong Li, Timothy J Mitchison

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 46 citations in OpenAlex.

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  6. Herpesviral replication compartments move and coalesce at nuclear speckles to enhance export of viral late mRNA.Proceedings of the National Academy of Sciences of the United States of America · 2011
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  10. Mechanical and spatial determinants of cytoskeletal geodesic dome formation in cardiac fibroblasts.Integrative biology : quantitative biosciences from nano to macro · 2009
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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

4 authors at 2 institutions in 1 country.

Justin C YarrowDept of Cell Biology, Harvard Medical School, 240 Longwood Ave, Boston, MA 02115, USA. jyarrow@hms.harvard.edu
Terry Lechler
Rong Li
Timothy J Mitchison
Harvard University · USHarvard Stem Cell Institute · US

Funding

Mechanisms of cell polarization in yeastR01GM057063 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI LI, RONG · 1998 to 2015
$5.3M
ACTIN DYNAMICS AND CELL LOCOMOTIONR01GM048027 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1992 to 2004
$1.8M
NIGMS NIH HHS GM057063NIGMS NIH HHS GM48027NIGMS NIH HHS R01 GM048027NIGMS NIH HHS R01 GM057063
6 · The paper itself

Abstract

background2,3-butanedione monoxime (BDM) has been widely used as a non-muscle myosin inhibitor to investigate the role of non-muscle myosinII in the process of actin retrograde flow and other actin cytoskeletal processes. Recent reports show that BDM does not inhibit any non-muscle myosins so far tested, including nm-myosinII, prompting the question, how were these process affected in BDM studies?

resultsWe have found that treatment of mammalian cells with BDM for only 1 min blocks actin incorporation at the leading edge in a permeabilized cell system. We show that inhibition of actin incorporation occurs through de-localization of leading edge proteins involved in actin polymerization--the Arp2/3 complex, WAVE, and VASP--that de-localize concomitantly with the leading edge actin network.

conclusionDe-localization of actin leading edge components by BDM treatment is a newly described effect of this compound. It may explain many of the results previously ascribed to inhibition of non-muscle myosinII by BDM, particularly in studies of leading edge dynamics. Though this effect of BDM is intriguing, future studies probing actin dynamics at the leading edge should use more potent and specific inhibitors.

Indexed as

Actin-Related Protein 3ActinsAnimalsCell Adhesion MoleculesCell LineCell Membrane PermeabilityChlorocebus aethiopsCytoskeletal ProteinsDiacetylKidneyMiceMicrofilament ProteinsMyosin Type IIPhosphoproteinsSwiss 3T3 CellsVasodilator-Stimulated PhosphoproteinActin-Related Protein 3ActinsActr3 protein, mouseCell Adhesion MoleculesCytoskeletal ProteinsDiacetyldiacetylmonoximeMicrofilament ProteinsMyosin Type IIPhosphoproteinsVasodilator-Stimulated PhosphoproteinWasf1 protein, mouseWiskott-Aldrich Syndrome Protein Family

Identifiers

PMID12783627
PMCPMC165424
OpenAlexW2120372267

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.