Evidence map›Paper›PMID 31451035›Full record

ArticleSmall GTPases2021

RhoG and Cdc42 can contribute to Rac-dependent lamellipodia formation through WAVE regulatory complex-binding.

Matthias Schaks, Hermann Döring, Frieda Kage, Anika Steffen, Thomas Klünemann, Wulf Blankenfeldt, Theresia Stradal, Klemens Rottner

Open access · hybridAbstract read
In one paragraph

Article in Small GTPases, 2021. 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
1.6field-weighted citation impact, top 17% 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, 17 citations in OpenAlex.

  1. Decoding Rho GTPase signalling networks in directed cell migration.Frontiers in cell and developmental biology · 2026
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  12. Actin dynamics in cell migration.Essays in biochemistry · 2019
    Review
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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

8 authors at 1 institution in 1 country.

Matthias SchaksDivision of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig , Braunschweig, Germany.ORCID 0000-0001-6362-7909
Hermann DöringDivision of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig , Braunschweig, Germany.ORCID 0000-0001-6699-8393
Frieda KageDivision of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig , Braunschweig, Germany.ORCID 0000-0002-9834-3946
Anika SteffenCell Biology, Helmholtz Centre for Infection Research , Braunschweig, Germany.ORCID 0000-0002-2933-0543
Thomas KlünemannStructure and Function of Proteins, Helmholtz Centre for Infection Research , Braunschweig, Germany.ORCID 0000-0002-2897-0936
Wulf BlankenfeldtStructure and Function of Proteins, Helmholtz Centre for Infection Research , Braunschweig, Germany.ORCID 0000-0001-9886-9668
Theresia StradalCell Biology, Helmholtz Centre for Infection Research , Braunschweig, Germany.ORCID 0000-0002-0352-9474
Klemens RottnerDivision of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig , Braunschweig, Germany.ORCID 0000-0003-4244-4198
Helmholtz Centre for Infection Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell migration frequently involves the formation of lamellipodial protrusions, the initiation of which requires Rac GTPases signalling to heteropentameric WAVE regulatory complex (WRC). While Rac-related RhoG and Cdc42 can potently stimulate lamellipodium formation, so far presumed to occur by upstream signalling to Rac activation, we show here that the latter can be bypassed by RhoG and Cdc42 given that WRC has been artificially activated. This evidence arises from generation of B16-F1 cells simultaneously lacking both Rac GTPases and WRC, followed by reconstitution of lamellipodia formation with specific Rho-GTPase and differentially active WRC variant combinations. We conclude that formation of canonical lamellipodia requires WRC activation through Rac, but can possibly be tuned, in addition, by WRC interactions with RhoG and Cdc42.

Indexed as

cdc42 GTP-Binding ProteinPseudopodiarho GTP-Binding ProteinsAnimalsMiceProtein Bindingrac GTP-Binding ProteinsSignal TransductionWiskott-Aldrich Syndrome Protein Familycdc42 GTP-Binding ProteinCdc42 protein, mouserac GTP-Binding ProteinsRhog protein, mouserho GTP-Binding ProteinsWiskott-Aldrich Syndrome Protein FamilyArp2/3 complexblebbingCRISPR/Cas9filopodiumlamellipodiummigrationprotrusionRho-GTPasestress fibre

Identifiers

PMID31451035
PMCPMC7849749
OpenAlexW2970996267

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.