Evidence map›Paper›PMID 28584191›Full record

ArticleJournal of cell science2017

ARHGAP42 is activated by Src-mediated tyrosine phosphorylation to promote cell motility.

Weifeng Luo, Radoslav Janoštiak, Ondřej Tolde, Larisa M Ryzhova, Lenka Koudelková, Michal Dibus, Jan Brábek, Steven K Hanks, Daniel Rosel

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2017. 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
1.0field-weighted citation impact, top 27% 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. Article
  2. Sex differences in synaptic plasticity underlying learning.Journal of neuroscience research · 2023
    Review
  3. Fixing the GAP: The role of RhoGAPs in cancer.European journal of cell biology · 2022
    Review
  4. Article
  5. Article
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  8. Article
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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

9 authors at 2 institutions in 2 countries.

Weifeng LuoDepartment of Cell Biology, Charles University in Prague, Viničná 7, Prague, 12843, Czech Republic.
Radoslav JanoštiakDepartment of Cell Biology, Charles University in Prague, Viničná 7, Prague, 12843, Czech Republic.
Ondřej ToldeDepartment of Cell Biology, Charles University in Prague, Viničná 7, Prague, 12843, Czech Republic.
Larisa M RyzhovaDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Lenka KoudelkováDepartment of Cell Biology, Charles University in Prague, Viničná 7, Prague, 12843, Czech Republic.
Michal DibusDepartment of Cell Biology, Charles University in Prague, Viničná 7, Prague, 12843, Czech Republic.
Jan BrábekDepartment of Cell Biology, Charles University in Prague, Viničná 7, Prague, 12843, Czech Republic.
Steven K HanksDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Daniel RoselDepartment of Cell Biology, Charles University in Prague, Viničná 7, Prague, 12843, Czech Republic rosel@natur.cuni.cz.ORCID http://orcid.org/0000-0001-7221-8672
Charles University · CZVanderbilt University · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI STACIE B DUSETZINA · 1995 to 2026
$172.8M
FUNCTIONAL STUDIES OF FOCAL ADHESION KINASER01GM049882 · NIGMS · VANDERBILT UNIVERSITY · PI HANKS, STEVEN K. · 1995 to 2010
$3.2M
NCI NIH HHS P30 CA068485NIGMS NIH HHS R01 GM049882
6 · The paper itself

Abstract

The tyrosine kinase Src acts as a key regulator of cell motility by phosphorylating multiple protein substrates that control cytoskeletal and adhesion dynamics. In an earlier phosphotyrosine proteomics study, we identified a novel Rho-GTPase activating protein, now known as ARHGAP42, as a likely biologically relevant Src substrate. ARHGAP42 is a member of a family of RhoGAPs distinguished by tandem BAR-PH domains lying N-terminal to the GAP domain. Like other family members, ARHGAP42 acts preferentially as a GAP for RhoA. We show that Src principally phosphorylates ARHGAP42 on tyrosine 376 (Tyr-376) in the short linker between the BAR-PH and GAP domains. The expression of ARHGAP42 variants in mammalian cells was used to elucidate its regulation. We found that the BAR domain is inhibitory toward the GAP activity of ARHGAP42, such that BAR domain deletion resulted in decreased active GTP-bound RhoA and increased cell motility. With the BAR domain intact, ARHGAP42 GAP activity could be activated by phosphorylation of Tyr-376 to promote motile cell behavior. Thus, phosphorylation of ARHGAP42 Tyr-376 is revealed as a novel regulatory event by which Src can affect actin dynamics through RhoA inhibition.

Indexed as

AnimalsCell MovementFocal AdhesionsGTPase-Activating ProteinsHumansMicePhosphorylationrhoA GTP-Binding Proteinrho GTP-Binding Proteinssrc-Family KinasesTyrosineARHGAP42 protein, humanGTPase-Activating ProteinsrhoA GTP-Binding ProteinRHOA protein, humanRhoA protein, mouserho GTP-Binding Proteinssrc-Family KinasesTyrosineFocal adhesionGAPGRAFMotilityRhoASrcTyrosine phosphorylation

Identifiers

PMID28584191
PMCPMC5536916
OpenAlexW2620584940

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.