Evidence map›Paper›PMID 24747073›Full record

ArticleBiochemical and biophysical research communications2014

A novel role for IQGAP1 protein in cell motility through cell retraction.

Sahar Foroutannejad, Nathan Rohner, Michael Reimer, Guim Kwon, Joseph M Schober

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. ERK signaling for cell migration and invasion.Frontiers in molecular biosciences · 2022
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
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  9. 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

5 authors at 1 institution in 1 country.

Sahar ForoutannejadDepartment of Pharmaceutical Sciences, Southern Illinois University School of Pharmacy, Edwardsville, IL 62026, USA.
Nathan RohnerDepartment of Pharmaceutical Sciences, Southern Illinois University School of Pharmacy, Edwardsville, IL 62026, USA.
Michael ReimerDepartment of Pharmaceutical Sciences, Southern Illinois University School of Pharmacy, Edwardsville, IL 62026, USA.
Guim KwonDepartment of Pharmaceutical Sciences, Southern Illinois University School of Pharmacy, Edwardsville, IL 62026, USA.
Joseph M SchoberDepartment of Pharmaceutical Sciences, Southern Illinois University School of Pharmacy, Edwardsville, IL 62026, USA. Electronic address: joschob@siue.edu.
Southern Illinois University Edwardsville · US

Funding

EB1 protein: regulator of actin protrusion and cell motilityR15GM093288 · NIGMS · SOUTHERN ILLINOIS UNIV AT EDWARDSVILLE · PI SCHOBER, JOSEPH MARTIN · 2011 to 2011
$215k
NIGMS NIH HHS R15 GM093288NIGMS NIH HHS R15GM093288
6 · The paper itself

Abstract

IQGAP1 has emerged as a key component in the regulation of cytoskeleton dynamics during cell migration, maintenance of adherens junctions, microbial pathogenesis and intracellular trafficking. IQGAP1 is known to localize to the protruding edge of lamellipodia in a variety of cell types and interact with regulators of actin dynamics. Here, we provide evidence suggesting a novel role of IQGAP1 in cell motility through cell edge retraction. In some of the cell lines examined, IQGAP1 was markedly separated from WAVE localization suggesting IQGAP1 may localize to retracting edges. B16F10 mouse melanoma cells exhibited the most restricted separation in which the appearance of GFP-IQGAP1 correlated with cell edge retraction velocity and the disappearance of mCherry-Arp3. These results demonstrate that in some cell types IQGAP1 may function to promote cell retraction not lamellipodium edge protrusion. In addition, we examined co-localization of IQGAP1 with adhesion site markers, myosin IIA, calmodulin and IQGAP2. In areas rich in IQGAP1 there was decreased immunofluorescence staining of vinculin, paxillin and phosphorylated-tyrosine indicating adhesion site disassembly. Interestingly, calmodulin, but not myosin IIA or IQGAP2, co-localized with IQGAP1 in areas of cell retraction. Overall these results suggest a new role of IQGAP1, distinct form IQGAP2, in cell migration through up regulation of contractility and downregulation of adhesion sites potentially through calmodulin interaction.

Indexed as

AnimalsCalmodulinCell AdhesionCell LineCell MovementMiceNonmuscle Myosin Type IIAPseudopodiaras GTPase-Activating ProteinsCalmodulinIqgap2 protein, mouseIQ motif containing GTPase activating protein 1Nonmuscle Myosin Type IIAras GTPase-Activating ProteinsActinCalmodulinCell adhesionCell retractionIQGAP1IQGAP2

Identifiers

PMID24747073
PMCPMC4052836
OpenAlexW2004931252

What OpenQuestion holds

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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.