Evidence map›Paper›PMID 18316075›Full record

ArticleExperimental cell research2008

RhoA/ROCK-mediated switching between Cdc42- and Rac1-dependent protrusion in MTLn3 carcinoma cells.

Mirvat El-Sibai, Olivier Pertz, Huan Pang, Shu-Chin Yip, Mike Lorenz, Marc Symons, John S Condeelis, Klaus M Hahn, Jonathan M Backer

Abstract read
In one paragraph

Article in Experimental cell research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

53 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
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  19. Gap Junctions and Wnt Signaling in the Mammary Gland: a Cross-Talk?Journal of mammary gland biology and neoplasia · 2019
    Review
  20. Article
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 4 institutions in 1 country.

Mirvat El-SibaiDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Olivier Pertz
Huan Pang
Shu-Chin Yip
Mike Lorenz
Marc Symons
John S Condeelis
Klaus M Hahn
Jonathan M Backer
Albert Einstein College of Medicine · USNorthwell Health · USScripps Research Institute · USUniversity of North Carolina at Chapel Hill · US

Funding

STRUCTUREU54GM064346 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI IMPERIALI, BARBARA · 2001 to 2010
$74.9M
Tumor Progression and MetastasisP01CA100324 · NCI · YESHIVA UNIVERSITY · PI CONDEELIS, JOHN S · 2003 to 2018
$30.0M
P85/P110 PI 3 KINASE--STRUCTURE/FUNCTION AND PHYSIOLOGYR01GM055692 · NIGMS · YESHIVA UNIVERSITY · PI BACKER, JONATHAN M. · 1997 to 2013
$4.4M
Signal transduction regulating tumor cell disseminationR01CA150344 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI CONDEELIS, JOHN S · 2010 to 2020
$3.7M
NCI NIH HHS CA 100324NCI NIH HHS P01 CA100324NCI NIH HHS R01 CA150344NIGMS NIH HHS GM64346NIGMS NIH HHS R01 GM055692NIGMS NIH HHS U54 GM064346
6 · The paper itself

Abstract

Rho GTPases are versatile regulators of cell shape that act on the actin cytoskeleton. Studies using Rho GTPase mutants have shown that, in some cells, Rac1 and Cdc42 regulate the formation of lamellipodia and filopodia, respectively at the leading edge, whereas RhoA mediates contraction at the rear of moving cells. However, recent reports have described a zone of RhoA/ROCK activation at the front of cells undergoing motility. In this study, we use a FRET-based RhoA biosensor to show that RhoA activation localizes to the leading edge of EGF-stimulated cells. Inhibition of Rho or ROCK enhanced protrusion, yet markedly inhibited cell motility; these changes correlated with a marked activation of Rac-1 at the cell edge. Surprisingly, whereas EGF-stimulated protrusion in control MTLn3 cells is Rac-independent and Cdc42-dependent, the opposite pattern is observed in MTLn3 cells after inhibition of ROCK. Thus, Rho and ROCK suppress Rac-1 activation at the leading edge, and inhibition of ROCK causes a switch between Cdc42 and Rac-1 as the dominant Rho GTPase driving protrusion in carcinoma cells. These data describe a novel role for Rho in coordinating signaling by Rac and Cdc42.

Indexed as

AmidesAnimalsCarcinomacdc42 GTP-Binding ProteinCell Line, TumorCell MembraneCell MovementEnzyme ActivationEnzyme InhibitorsEpidermal Growth FactorFocal AdhesionsHumansProtein TransportPseudopodiaPyridinesrac1 GTP-Binding ProteinAmidescdc42 GTP-Binding ProteinEnzyme InhibitorsEpidermal Growth FactorPyridinesrac1 GTP-Binding ProteinrhoA GTP-Binding Proteinrho-Associated KinasesY 27632

Identifiers

PMID18316075
PMCPMC2677995
OpenAlexW2070765312

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.