Evidence map›Paper›PMID 34830479›Full record

ArticleInternational journal of molecular sciences2021

Selectivity Determinants of RHO GTPase Binding to IQGAPs.

Niloufar Mosaddeghzadeh, Kazem Nouri, Oliver H F Krumbach, Ehsan Amin, Radovan Dvorsky, Mohammad R Ahmadian

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

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  4. The Role of the Swollen State in Cell Proliferation.The Journal of membrane biology · 2025
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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

6 authors at 1 institution in 2 countries.

Niloufar MosaddeghzadehMedical Faculty, Institute of Biochemistry and Molecular Biology II, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0001-5786-8992
Kazem NouriMedical Faculty, Institute of Biochemistry and Molecular Biology II, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Oliver H F KrumbachMedical Faculty, Institute of Biochemistry and Molecular Biology II, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Ehsan AminMedical Faculty, Institute of Biochemistry and Molecular Biology II, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0003-2995-8864
Radovan DvorskyMedical Faculty, Institute of Biochemistry and Molecular Biology II, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Mohammad R AhmadianMedical Faculty, Institute of Biochemistry and Molecular Biology II, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0002-2034-8894
Düsseldorf University Hospital · DE

Funding

Deutsche Forschungsgemeinschaft grant number: AH 92/8-1Deutsche Forschungsgemeinschaft grant number: IRTG 1902-p6Federal Ministry of Education and Research GeNeRARe, grant numbers: 01GM1902Cthe European Network on Noonan Syndrome and Related Disorders NSEuroNet, grant number: 01GM1621B
6 · The paper itself

Abstract

IQ motif-containing GTPase-activating proteins (IQGAPs) modulate a wide range of cellular processes by acting as scaffolds and driving protein components into distinct signaling networks. Their functional states have been proposed to be controlled by members of the RHO family of GTPases, among other regulators. In this study, we show that IQGAP1 and IQGAP2 can associate with CDC42 and RAC1-like proteins but not with RIF, RHOD, or RHO-like proteins, including RHOA. This seems to be based on the distribution of charged surface residues, which varies significantly among RHO GTPases despite their high sequence homology. Although effector proteins bind first to the highly flexible switch regions of RHO GTPases, additional contacts outside are required for effector activation. Sequence alignment and structural, mutational, and competitive biochemical analyses revealed that RHO GTPases possess paralog-specific residues outside the two highly conserved switch regions that essentially determine the selectivity of RHO GTPase binding to IQGAPs. Amino acid substitution of these specific residues in RHOA to the corresponding residues in RAC1 resulted in RHOA association with IQGAP1. Thus, electrostatics most likely plays a decisive role in these interactions.

Indexed as

Amino Acid SubstitutionBinding Sitescdc42 GTP-Binding ProteinHumansMutationProtein Bindingrac1 GTP-Binding Proteinras GTPase-Activating ProteinsrhoA GTP-Binding Proteinrho GTP-Binding ProteinsSequence Alignmentcdc42 GTP-Binding ProteinCDC42 protein, humanIQGAP2 protein, humanIQ motif containing GTPase activating protein 1rac1 GTP-Binding Proteinras GTPase-Activating ProteinsrhoA GTP-Binding ProteinRHOA protein, humanrho GTP-Binding ProteinsCDC42IQGAPRAC1RHO GTPasesscaffoldselective bindings

Identifiers

PMID34830479
PMCPMC8625570
OpenAlexW3216093367

What OpenQuestion holds

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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.