Evidence map›Paper›PMID 19862699›Full record

ReviewJournal of cellular biochemistry2009

The cofilin activity cycle in lamellipodia and invadopodia.

Matthew Oser, John Condeelis

Open access · greenAbstract readReview
In one paragraph

Review in Journal of cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

109 citing papers in PubMed, 184 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. International journal of environmental research and public health · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Functional Role of Non-Muscle Myosin II in Microglia: An Updated Review.International journal of molecular sciences · 2021
    Review
  15. Review
  16. The Plasma Membrane CaCancers · 2021
    Article
  17. Article
  18. Knockout ofInternational journal of molecular sciences · 2020
    Article
  19. Article
  20. Review

49 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

2 authors at 2 institutions in 1 country.

Matthew OserDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine of Yeshiva University, Bronx, New York 10461, USA. moser@aecom.yu.edu
John Condeelis
Albert Einstein College of Medicine · USYeshiva University · US

Funding

STRUCTUREU54GM064346 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI IMPERIALI, BARBARA · 2001 to 2010
$74.9M
Tumor Progression and MetastasisP01CA100324 · NCI · YESHIVA UNIVERSITY · PI CONDEELIS, JOHN S · 2003 to 2018
$30.0M
SIGNAL TRANSDUCTION AND ACTIN DURING AMOEBOID CHEMOTAXISR01GM038511 · NIGMS · YESHIVA UNIVERSITY · PI CONDEELIS, JOHN S · 1988 to 2008
$2.8M
Novel Methods for Detecting Cell Interactions in the Tumor MicroenvironmentU54CA126511 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI CONDEELIS, JOHN S · 2006 to 2010
$2.2M
NCI NIH HHS CA100324NCI NIH HHS CA126511NCI NIH HHS P01 CA100324NCI NIH HHS U54 CA126511NIGMS NIH HHS GM064346NIGMS NIH HHS GM38511NIGMS NIH HHS R01 GM038511NIGMS NIH HHS U54 GM064346
6 · The paper itself

Abstract

The actin severing protein cofilin is essential for directed cell migration and chemotaxis, in many cell types and is also important for tumor cell invasion during metastasis. Through its severing activity, cofilin increases the number of free barbed ends to initiate actin polymerization for actin-based protrusion in two distinct subcellular compartments in invasive tumor cells: lamellipodia and invadopodia. Cofilin severing activity is tightly regulated and multiple mechanisms are utilized to regulate cofilin activity. In this prospect, we have grouped the primary on/off regulation into two broad categories, both of which are important for inhibiting cofilin from binding to F-actin or G-actin: (1) Blocking cofilin activity by the binding of cofilin to either PI(4,5)P(2) at lamellipodia, or cortactin at invadopodia. (2) Blocking cofilin's ability to bind to actin via serine phosphorylation. Although the literature suggests that these cofilin regulatory mechanisms may be cell-type dependent, we propose the existence of a common cofilin activity cycle in which both operate. In this common cycle, the mechanism used to initiate cofilin activity is determined by the starting point in the cycle in a given subcellular compartment.

Indexed as

Actin Depolymerizing FactorsActinsAnimalsCell MovementHumansPhosphorylationPseudopodiaSerineActin Depolymerizing FactorsActinsSerine

Identifiers

PMID19862699
PMCPMC3718474
OpenAlexW2098301459

What OpenQuestion holds

Textmetadata
LicenceTDM
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.