Evidence map›Paper›PMID 23760270›Full record

ArticleThe Journal of biological chemistry2013

ArhGAP15, a Rac-specific GTPase-activating protein, plays a dual role in inhibiting small GTPase signaling.

Maria Radu, Sonali J Rawat, Alexander Beeser, Anton Iliuk, Weiguo Andy Tao, Jonathan Chernoff

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.9field-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

22 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Patterning of the cell cortex by Rho GTPases.Nature reviews. Molecular cell biology · 2024
    Review
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  6. Review
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  8. Article
  9. Review
  10. Etiopathogenetic Mechanisms in Diverticular Disease of the Colon.Cellular and molecular gastroenterology and hepatology · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
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  19. Article
  20. Review
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

6 authors at 3 institutions in 1 country.

Maria RaduFrom the Cancer Biology Program, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111.
Sonali J Rawatthe Department of Biochemistry and Molecular Biology, Drexel University, Philadelphia, Pennsylvania 19102, and.
Alexander BeeserFrom the Cancer Biology Program, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111.
Anton Iliukthe Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
Weiguo Andy Taothe Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
Jonathan ChernoffFrom the Cancer Biology Program, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111,. Electronic address: Jonathan.Chernoff@fccc.edu.
Fox Chase Cancer Center · USPurdue University West Lafayette · USDrexel University · US

Funding

WORD PROCESSING CENTER--COREP30CA006927 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI Margaret von Mehren · 1985 to 2026
$138.8M
TRAINING PROGRAM IN CANCER RESEARCHT32CA009035 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI CHERNOFF, JONATHAN · 1985 to 2020
$10.5M
Targeting the Kinome in Neurofibromatosis type 1R01CA142928 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI CHERNOFF, JONATHAN · 2010 to 2019
$3.9M
Early events of carcinoma induced by ErbB receptorsR01CA098830 · NCI · COLD SPRING HARBOR LABORATORY · PI MUTHUSWAMY, SENTHIL K · 2003 to 2013
$3.4M
TUMOR-SUPPRESSING PROTEIN-TYROSINE PHOSPHATASER01CA058836 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI CHERNOFF, JONATHAN D. · 1993 to 2007
$3.0M
New Proteomic Technologies for the Analysis of Tyrosine Kinase Signaling PathwaysR01GM088317 · NIGMS · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2010 to 2014
$1.6M
NCI NIH HHS P30 CA006927NCI NIH HHS R01 CA058836NCI NIH HHS R01 CA098830NCI NIH HHS R01 CA142928NCI NIH HHS R01 CA58836NCI NIH HHS T32 CA009035NIGMS NIH HHS R01 GM088317
6 · The paper itself

Abstract

Signaling from small GTPases is a tightly regulated process. In this work we used a protein microarray screen to identify the Rac-specific GAP, ArhGAP15, as a substrate of the Rac effectors Pak1 and Pak2. In addition to serving as a substrate of Pak1/2, we found that ArhGAP15, via its PH domain, bound to these kinases. The association of ArhGAP15 to Pak1/2 resulted in mutual inhibition of GAP and kinase catalytic activity, respectively. Knock-down of ArhGAP15 resulted in activation of Pak1/2, both indirectly, as a result of Rac activation, and directly, as a result of disruption of the ArhGAP15/Pak complex. Our data suggest that ArhGAP15 plays a dual negative role in regulating small GTPase signaling, by acting at the level of the GTPase itself, as well interacting with its effector, Pak kinase.

Indexed as

Signal TransductionAmino Acid SequenceDown-RegulationExtracellular Signal-Regulated MAP KinasesGTPase-Activating ProteinsHEK293 CellsHumansMAP Kinase Signaling SystemModels, BiologicalMolecular Sequence Datap21-Activated KinasesPhosphorylationProtein BindingProtein Structure, Tertiaryrac GTP-Binding ProteinsSubstrate SpecificityARHGAP15 protein, humanExtracellular Signal-Regulated MAP KinasesGTPase-Activating Proteinsp21-Activated Kinasesrac GTP-Binding ProteinsERKProtein KinasesProtein PhosphorylationSignal TransductionSmall GTPases

Identifiers

PMID23760270
PMCPMC3774378
OpenAlexW1983086543

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.