Evidence map›Paper›PMID 19151751›Full record

ArticleOncogene2009

p120Ras-GAP binds the DLC1 Rho-GAP tumor suppressor protein and inhibits its RhoA GTPase and growth-suppressing activities.

X-Y Yang, M Guan, D Vigil, C J Der, D R Lowy, N C Popescu

Open access · bronzeAbstract read
In one paragraph

Article in Oncogene, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 65 citations in OpenAlex.

  1. Trial
  2. Article
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  4. Review
  5. Clinically observedbioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. RhoA: a dubious molecule in cardiac pathophysiology.Journal of biomedical science · 2021
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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  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 2 countries.

X-Y YangLaboratory of Experimental Carcinogenesis, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892-4262, USA.
M Guan
D Vigil
C J Der
D R Lowy
N C Popescu
Center for Cancer Research · USUniversity of North Carolina at Chapel Hill · USFudan University · CN

Funding

Tumor gene expression in vitro and in vivoZIABC008905 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI LOWY, DOUGLAS R. · 2009 to 2025
$14.3M
Molecular Cytogenetics of Solid TumorsZIABC010038 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI POPESCU, NICOLAE · 2009 to 2012
$4.5M
MOLECULAR CYTOGENETICS OF SOLID TUMORSZ01BC010038 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI POPESCU, NICOLAE · 1996 to 2008
$2.3M
Mechanism and role of DLC-1 tumor suppressor loss in lung cancerR01CA129610 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DER, CHANNING J. · 2008 to 2012
$1.5M
Intramural NIH HHS Z01 BC010038Intramural NIH HHS Z99 CA999999NCI NIH HHS 1R01CA129610NCI NIH HHS R01 CA129610
6 · The paper itself

Abstract

DLC1 (deleted in liver cancer 1), which encodes a Rho GTPase-activating protein (Rho-GAP), is a potent tumor suppressor gene that is frequently inactivated in several human cancers. DLC1 is a multidomain protein that has been shown previously to bind members of the tensin gene family. Here we show that p120Ras-GAP (Ras-GAP; also known as RASA1) interacts and extensively colocalizes with DLC1 in focal adhesions. The binding was mapped to the SH3 domain located in the N terminus of Ras-GAP and to the Rho-GAP catalytic domain located in the C terminus of the DLC1. In vitro analyses with purified proteins determined that the isolated Ras-GAP SH3 domain inhibits DLC1 Rho-GAP activity, suggesting that Ras-GAP is a negative regulator of DLC1 Rho-GAP activity. Consistent with this possibility, we found that ectopic overexpression of Ras-GAP in a Ras-GAP-insensitive tumor line impaired the growth-suppressing activity of DLC1 and increased RhoA activity in vivo. Our observations expand the complexity of proteins that regulate DLC1 function and define a novel mechanism of the cross talk between Ras and Rho GTPases.1R01CA129610

Indexed as

Catalytic DomainCell Line, TumorCell ProliferationGTPase-Activating ProteinsHumansNeoplasmsp120 GTPase Activating ProteinrhoA GTP-Binding Proteinsrc Homology DomainsTumor Suppressor ProteinsDLC1 protein, humanGTPase-Activating Proteinsp120 GTPase Activating ProteinrhoA GTP-Binding ProteinRHOA protein, humanTumor Suppressor Proteins

Identifiers

PMID19151751
PMCPMC2715999
OpenAlexW1985000689

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.