Evidence map›Paper›PMID 26427649›Full record

ArticleBiochimica et biophysica acta2015

Tensin1 positively regulates RhoA activity through its interaction with DLC1.

Yi-Ping Shih, Peng Sun, Aifeng Wang, Su Hao Lo

Erratum issuedAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

38 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Genes · 2023
    Article
  14. The molecular and clinical role of Tensin 1/2/3 in cancer.Journal of cellular and molecular medicine · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. miR-31-5p modulates cell progression in lung adenocarcinoma through TNS1/p53 axis.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2022
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Yi-Ping ShihDepartment of Biochemistry and Molecular Medicine, University of California-Davis, Sacramento, CA 95817, USA. Electronic address: ypshih@ucdavis.edu.
Peng SunDepartment of Biochemistry and Molecular Medicine, University of California-Davis, Sacramento, CA 95817, USA.
Aifeng WangDepartment of Biochemistry and Molecular Medicine, University of California-Davis, Sacramento, CA 95817, USA.
Su Hao LoDepartment of Biochemistry and Molecular Medicine, University of California-Davis, Sacramento, CA 95817, USA.
University of California, Davis · US

Funding

Training Program in Oncogenic Signals and Chromosome BiologyT32CA108459 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI HEYER, WOLF-DIETRICH · 2006 to 2020
$3.6M
Role of Cten in Prostate CancerR01CA102537 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI LO, SU HAO · 2004 to 2016
$2.4M
Mechanism of DLC1-mediated tumor suppressionR01CA151366 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LO, SU HAO · 2010 to 2014
$1.5M
Deleted in liver cancer 1 (DLC1) in liver development and diseaseK01DK097291 · NIDDK · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SHIH, YI-PING · 2013 to 2016
$471k
Role of Cten in Prostate CancerR56CA102537 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LO, SU HAO · 2009 to 2009
$240k
NCI NIH HHS CA102537NCI NIH HHS CA151366NCI NIH HHS R01 CA102537NCI NIH HHS R01 CA151366NCI NIH HHS R56 CA102537NCI NIH HHS T32 CA108459NIDDK NIH HHS DK097291NIDDK NIH HHS K01 DK097291
6 · The paper itself

Abstract

DLC1 is a RhoGAP-containing tumor suppressor and many of DLC1's functions are absolutely dependent on its RhoGAP activity. Through its RhoGAP domain, DLC1 inhibits the activity of RhoA GTPase, which regulates actin cytoskeleton networks and dis/assembly of focal adhesions. Tensin1 (TNS1) is a focal adhesion molecule that links the actin cytoskeleton to integrins and forms signaling complexes through its multiple binding domains. Here, we report that TNS1 enhances RhoA activity in a DLC1-dependent manner. This is accomplished by binding to DLC1 through TNS1's C2, SH2, and PTB domains. Point mutations at these three sites disrupt TNS1's interaction with DLC1 as well as its effect on RhoA activity. The biological relevance of this TNS1-DLC1-RhoA signaling axis is investigated in TNS1 knockout (KO) cells and mice. Endothelial cells isolated from TNS1 KO mice or those silenced with TNS1 siRNA show significant reduction in proliferation, migration, and tube formation activities. Concomitantly, the RhoA activity is down-regulated in TNS1 KO cells and this reduction is restored by further silencing of DLC1. Furthermore, the angiogenic process is compromised in TNS1 KO mice. These studies demonstrate that TNS1 binds to DLC1 and fine-tunes its RhoGAP activity toward RhoA and that the TNS1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis.

Indexed as

Amino Acid SequenceAnimalsBinding SitesGTPase-Activating ProteinsHuman Umbilical Vein Endothelial CellsMiceMice, KnockoutMicrofilament ProteinsMolecular Sequence DataProtein BindingrhoA GTP-Binding ProteinSequence Homology, Amino AcidTensinsTumor Suppressor ProteinsDLC-1 (deleted in liver cancer) protein, mouseGTPase-Activating ProteinsMicrofilament ProteinsrhoA GTP-Binding ProteinTensinsTNS1 protein, humanTns1 protein, mouseTumor Suppressor ProteinsAngiogenesisDLC1Focal adhesionRhoATensin

Identifiers

PMID26427649
PMCPMC4621260
OpenAlexW1787824584

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.