Evidence map›Paper›PMID 21730051›Full record

ArticleThe Journal of biological chemistry2011

The IQGAP1 protein is a calmodulin-regulated barbed end capper of actin filaments: possible implications in its function in cell migration.

Andrea Pelikan-Conchaudron, Christophe Le Clainche, Dominique Didry, Marie-France Carlier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Queue Gaps Among the IQGAPs inInternational journal of molecular sciences · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Selectivity Determinants of RHO GTPase Binding to IQGAPs.International journal of molecular sciences · 2021
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Site-specific expression of IQGAP1 in human nephrons.Journal of molecular histology · 2019
    Article
  17. Ras GTPase-Activating-Like Protein IQGAP1 (IQGAP1) Promotes Breast Cancer Proliferation and Invasion and Correlates with Poor Clinical Outcomes.Medical science monitor : international medical journal of experimental and clinical research · 2018
    Article
  18. Article
  19. Article
  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

4 authors at 2 institutions in 1 country.

Andrea Pelikan-ConchaudronCytoskeleton Dynamics and Motility group, UPR 3289, Laboratoire d'Enzymologie et Biochimie Structurale, CNRS, 91198 Gif-sur-Yvette, France.
Christophe Le Clainche
Dominique Didry
Marie-France Carlier
Laboratoire d'Enzymologie et Biochimie Structurales · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

IQGAP1 is a large modular protein that displays multiple partnership and is thought to act as a scaffold in coupling cell signaling to the actin and microtubule cytoskeletons in cell migration, adhesion, and cytokinesis. However the molecular mechanisms underlying the activities of IQGAP1 are poorly understood in part because of its large size, poor solubility and lack of functional assays to challenge biochemical properties in various contexts. We have purified bacterially expressed recombinant human IQGAP1. The protein binds Cdc42, Rac1, and the CRIB domain of N-WASP in a calmodulin-sensitive fashion. We further show that in addition to bundling of filaments via a single N-terminal calponin-homology domain, IQGAP1 actually regulates actin assembly. It caps barbed ends, with a higher affinity for ADP-bound terminal subunits (K(B) = 4 nM). The barbed end capping activity is inhibited by calmodulin, consistent with calmodulin binding to IQGAP1 with a K(C) of 40 nm, both in the absence and presence of Ca(2+) ions. The barbed end capping activity resides in the C-terminal half of IQGAP1. It is possible that the capping activity of IQGAP1 accounts for its stimulation of cell migration. We further find that bacterially expressed recombinant IQGAP1 fragments easily co-purify with nucleic acids that turn out to activate N-WASP protein to branch filaments with Arp2/3 complex. The present results open perspectives for tackling the function of IQGAP1 in more complex reconstituted systems.

Indexed as

ActinsAdenosine DiphosphateCalmodulincdc42 GTP-Binding ProteinCell MovementDNA, ComplementaryHumansKineticsPoint MutationProtein BindingProtein Structure, Tertiaryras GTPase-Activating ProteinsRecombinant ProteinsSignal TransductionSolubilityWiskott-Aldrich Syndrome Protein, NeuronalActinsAdenosine DiphosphateCalmodulincdc42 GTP-Binding ProteinDNA, ComplementaryIQ motif containing GTPase activating protein 1ras GTPase-Activating ProteinsRecombinant ProteinsWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID21730051
PMCPMC3186398
OpenAlexW2052224433

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.