Evidence map›Paper›PMID 36012107›Full record

ArticleInternational journal of molecular sciences2022

CDC42-IQGAP Interactions Scrutinized: New Insights into the Binding Properties of the GAP-Related Domain.

Niloufar Mosaddeghzadeh, Silke Pudewell, Farhad Bazgir, Neda S Kazemein Jasemi, Oliver H F Krumbach, Lothar Gremer, Dieter Willbold, Radovan Dvorsky, Mohammad R Ahmadian

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Article
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  3. Review
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  5. Review
  6. Article
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  8. 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

9 authors.

Niloufar MosaddeghzadehInstitute of Biochemistry and Molecular Biology II, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0001-5786-8992
Silke PudewellInstitute of Biochemistry and Molecular Biology II, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0002-4653-7263
Farhad BazgirInstitute of Biochemistry and Molecular Biology II, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0002-0689-7926
Neda S Kazemein JasemiInstitute of Biochemistry and Molecular Biology II, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Oliver H F KrumbachInstitute of Biochemistry and Molecular Biology II, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Lothar GremerInstitute of Physical Biology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0001-7065-5027
Dieter WillboldInstitute of Physical Biology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0002-0065-7366
Radovan DvorskyInstitute of Biochemistry and Molecular Biology II, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Mohammad R AhmadianInstitute of Biochemistry and Molecular Biology II, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0002-2034-8894

Funding

Deutsche Forschungsgemeinschaft IRTG 1902-p6Federal Ministry of Education and Research 01GM1902Cthe European Network on Noonan Syndrome and Related Disorders (NSEuroNet) 01GM1621Bthe Operational Program Integrated Infrastructure ERDF: Open scientific community for modern interdisciplinary research in medicine (OPENMED) ITMS2014+: 313011V455the Research Committee of the Medical Faculty of the Heinrich Heine University 9772764
6 · The paper itself

Abstract

The IQ motif-containing GTPase-activating protein (IQGAP) family composes of three highly-related and evolutionarily conserved paralogs (IQGAP1, IQGAP2 and IQGAP3), which fine tune as scaffolding proteins numerous fundamental cellular processes. IQGAP1 is described as an effector of CDC42, although its effector function yet re-mains unclear. Biophysical, biochemical and molecular dynamic simulation studies have proposed that IQGAP RASGAP-related domains (GRDs) bind to the switch regions and the insert helix of CDC42 in a GTP-dependent manner. Our kinetic and equilibrium studies have shown that IQGAP1 GRD binds, in contrast to its C-terminal 794 amino acids (called C794), CDC42 in a nucleotide-independent manner indicating a binding outside the switch regions. To resolve this discrepancy and move beyond the one-sided view of GRD, we carried out affinity measurements and a systematic mutational analysis of the interfacing residues between GRD and CDC42 based on the crystal structure of the IQGAP2 GRD-CDC42

Indexed as

cdc42 GTP-Binding Proteinras GTPase-Activating ProteinsBinding SitesGTPase-Activating ProteinsGuanosine TriphosphateNucleotidesProtein Bindingcdc42 GTP-Binding ProteinGTPase-Activating ProteinsGuanosine TriphosphateNucleotidesras GTPase-Activating ProteinsCDC42GAPGAP-related domainGRDGTPase activating proteinIQGAPnucleotide-independent bindingRASGAPRHO GTPasesscaffolding proteinscaffold proteinswitch regions

Identifiers

PMID36012107
PMCPMC9408373

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Registered trials

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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.