Evidence map›Paper›PMID 30914742›Full record

ArticleScientific reports2019

The small GTPase RhoG regulates microtubule-mediated focal adhesion disassembly.

Ashtyn Zinn, Silvia M Goicoechea, Gabriel Kreider-Letterman, Debonil Maity, Sahezeel Awadia, Luis Cedeno-Rosario, Yun Chen, Rafael Garcia-Mata

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Multi-omic Profiling of Recurrence Risk Across Breast Cancer Subtypes.medRxiv : the preprint server for health sciences · 2026
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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

8 authors at 2 institutions in 1 country.

Ashtyn ZinnDepartment of Biological Sciences, University of Toledo, 2801 W. Bancroft St., MS601, BO3090, Toledo, OH, 43606, USA.
Silvia M GoicoecheaDepartment of Biological Sciences, University of Toledo, 2801 W. Bancroft St., MS601, BO3090, Toledo, OH, 43606, USA.
Gabriel Kreider-LettermanDepartment of Biological Sciences, University of Toledo, 2801 W. Bancroft St., MS601, BO3090, Toledo, OH, 43606, USA.
Debonil MaityJohns Hopkins University, Department of Mechanical Engineering, Latrobe Hall 223, 3400 North Charles St., Baltimore, MD, 21218, USA.
Sahezeel AwadiaDepartment of Biological Sciences, University of Toledo, 2801 W. Bancroft St., MS601, BO3090, Toledo, OH, 43606, USA.
Luis Cedeno-RosarioDepartment of Biological Sciences, University of Toledo, 2801 W. Bancroft St., MS601, BO3090, Toledo, OH, 43606, USA.
Yun ChenJohns Hopkins University, Department of Mechanical Engineering, Latrobe Hall 223, 3400 North Charles St., Baltimore, MD, 21218, USA.
Rafael Garcia-MataDepartment of Biological Sciences, University of Toledo, 2801 W. Bancroft St., MS601, BO3090, Toledo, OH, 43606, USA. rafael.garciamata@utoledo.edu.
University of Toledo · USJohns Hopkins University · US

Funding

Regulation of Invadopodia Formation by RhoG Specific GEFs and GAPsR15CA199101 · NCI · UNIVERSITY OF TOLEDO · PI GARCIA-MATA, RAFAEL · 2016 to 2016
$409k
RhoG Signaling in InvadopodiaR21CA194776 · NCI · UNIVERSITY OF TOLEDO · PI GARCIA-MATA, RAFAEL · 2016 to 2017
$331k
A Novel RhoG Protein Interaction Network in InvadopodiaR03CA197227 · NCI · UNIVERSITY OF TOLEDO · PI GARCIA-MATA, RAFAEL · 2016 to 2017
$151k
NCI NIH HHS R03 CA197227NCI NIH HHS R15 CA199101NCI NIH HHS R21 CA194776
6 · The paper itself

Abstract

Focal adhesions (FA) are a complex network of proteins that allow the cell to form physical contacts with the extracellular matrix (ECM). FA assemble and disassemble in a dynamic process, orchestrated by a variety of cellular components. However, the underlying mechanisms that regulate adhesion turnover remain poorly understood. Here we show that RhoG, a Rho GTPase related to Rac, modulates FA dynamics. When RhoG expression is silenced, FA are more stable and live longer, resulting in an increase in the number and size of adhesions, which are also more mature and fibrillar-like. Silencing RhoG also increases the number and thickness of stress fibers, which are sensitive to blebbistatin, suggesting contractility is increased. The molecular mechanism by which RhoG regulates adhesion turnover is yet to be characterized, but our results demonstrate that RhoG plays a role in the regulation of microtubule-mediated FA disassembly.

Indexed as

ActomyosinCell Line, TumorCell ShapeFocal AdhesionsGene Knockdown TechniquesGene SilencingHumansMicrotubulesPseudopodiarho GTP-Binding ProteinsStress FibersActomyosinRHOG protein, humanrho GTP-Binding Proteins

Identifiers

PMID30914742
PMCPMC6435757
OpenAlexW2923986317

What OpenQuestion holds

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LicenceCC BY
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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.