Evidence map›Paper›PMID 20351273›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

An unconventional myosin required for cell polarization and chemotaxis.

Laura M Breshears, Deborah Wessels, David R Soll, Margaret A Titus

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Cells · 2022
    Article
  2. Adhesion ofFrontiers in cell and developmental biology · 2022
    Review
  3. Review
  4. Article
  5. MyTH4-FERM myosins have an ancient and conserved role in filopod formation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  6. Myosin-X and disease.Experimental cell research · 2015
    Review
  7. Article
  8. Article
  9. Article
  10. Myosin-X functions in polarized epithelial cells.Molecular biology of the cell · 2012
    Article
  11. Structural and functional insights on the Myosin superfamily.Bioinformatics and biology insights · 2012
    Article
  12. Review
  13. Article
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.

Laura M BreshearsDepartment of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, MN 55455, USA.
Deborah Wessels
David R Soll
Margaret A Titus
University of Iowa · USUniversity of Minnesota · US

Funding

DEVELOPMENTAL BIOLOGY TRAINING PROGRAMT32HD007480 · NICHD · UNIVERSITY OF MINNESOTA TWIN CITIES · PI O'CONNOR, MICHAEL BRENDAN · 1995 to 2011
$1.2M
NICHD NIH HHS T32 HD007480NICHD NIH HHS T32-HD007480
6 · The paper itself

Abstract

MyTH/FERM (myosin tail homology 4/band 4.1, ezrin, radixin, and moesin) myosins have roles in cellular adhesion, extension of actin-filled projections such as filopodia and stereocilia, and directional migration. The amoeba Dictyostelium discoideum expresses a simple complement of MyTH/FERM myosins, a class VII (M7) myosin required for cell-substrate adhesion and a unique myosin named MyoG. Mutants lacking MyoG exhibit a wide range of normal actin-based behaviors, including chemotaxis to folic acid, but have a striking defect in polarization and chemotaxis to cAMP. Although the myoG mutants respond to cAMP stimulation by increasing persistence and weakly increasing levels of cortical F-actin, they do not polarize; instead, they maintain a round shape and move slowly and randomly when exposed to a chemotactic gradient. The mutants also fail to activate and localize PI3K to the membrane closest to the source of chemoattractant. These data reveal a role for a MyTH/FERM myosin in mediating early chemotactic signaling and suggest that MyTH/FERM proteins have conserved roles in signaling and the generation of cell polarity.

Indexed as

ActinsAnimalsCell MovementChemotaxisCytoskeletonDictyosteliumGreen Fluorescent ProteinsModels, BiologicalMyogeninMyosinsPhenotypePhosphatidylinositol 3-KinasesProtein Structure, TertiarySignal TransductionActinsGreen Fluorescent ProteinsMyogeninMyosinsPhosphatidylinositol 3-Kinases

Identifiers

PMID20351273
PMCPMC2872422
OpenAlexW2030207567

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.