Evidence map›Paper›PMID 19158339›Full record

ArticleJournal of cell science2009

A common cofilin activity cycle in invasive tumor cells and inflammatory cells.

Jacco van Rheenen, John Condeelis, Michael Glogauer

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

71 citing papers in PubMed, 116 citations in OpenAlex.

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  9. Inositol Polyphosphate-5-Phosphatase K (The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
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  18. Study ofJournal of gastrointestinal oncology · 2018
    Article
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11 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

3 authors at 3 institutions in 3 countries.

Jacco van RheenenDepartment of Anatomy and Structural Biology, Gruss Lipper Center for Biophotonics, Albert Einstein College of Medicine of Yeshiva University, Bronx, NY 10461, USA. j.vanrheenen@niob.knaw.nl
John Condeelis
Michael Glogauer
Albert Einstein College of Medicine · USHubrecht Institute for Developmental Biology and Stem Cell Research · NLUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In many cell types, the formation of membrane protrusions and directional migration depend on the spatial and temporal regulation of the actin-binding protein cofilin. Cofilin, which is important for the regulation of actin-polymerization initiation, increases the number of actin free barbed ends through three mechanisms: its intrinsic actin-nucleation activity; binding and severing of existing actin filaments; and recycling actin monomers from old filaments to new ones through its actin-depolymerization activity. The increase in free barbed ends that is caused by cofilin initiates new actin polymerization, which can be amplified by the actin-nucleating ARP2/3 complex. Interestingly, different cell systems seem to have different mechanisms of activating cofilin. The initial activation of cofilin in mammary breast tumors is dependent on PLCgamma, whereas cofilin activation in neutrophils is additionally dependent on dephosphorylation, which is promoted through Rac2 signaling. Although the literature seems to be confusing and inconsistent, we propose that all of the data can be explained by a single activity-cycle model. In this Opinion, we give an overview of cofilin activation in both tumor cells and inflammatory cells, and demonstrate how the differences in cofilin activation that are observed in various cell types can be explained by different starting points in this single common activity cycle.

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsActinsAnimalsChemotaxisHumansInflammationNeoplasm InvasivenessNeoplasmsPhosphatidylinositol 4,5-DiphosphatePhospholipase C gammaPhosphorylationProtein KinasesActin Depolymerizing FactorsActinsPhosphatidylinositol 4,5-DiphosphatePhospholipase C gammaProtein Kinases

Identifiers

PMID19158339
PMCPMC2772875
OpenAlexW2044785751

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.