Evidence map›Paper›PMID 22279049›Full record

ArticleGenes & development2012

IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling.

Nadine Stöhr, Marcel Köhn, Marcell Lederer, Markus Glass, Claudia Reinke, Robert H Singer, Stefan Hüttelmaier

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing 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

96 citing papers in PubMed, 180 citations in OpenAlex.

  1. The cellular landscape of druggable RNA-binding proteins.Nature reviews. Drug discovery · 2026
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  16. IGF2BPs as novel mGenes & diseases · 2024
    Review
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  20. Review

36 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 2 countries.

Nadine StöhrSection for Molecular Cell Biology, Institute of Molecular Medicine, Martin Luther University of Halle, Halle, Germany.
Marcel Köhn
Marcell Lederer
Markus Glass
Claudia Reinke
Robert H Singer
Stefan Hüttelmaier
Martin Luther University Halle-Wittenberg · DEAlbert Einstein College of Medicine · US

Funding

MECHANISM OF ACTIN MRNA LOCALIZATIONR01AR041480 · NIAMS · YESHIVA UNIVERSITY · PI SINGER, ROBERT H · 1992 to 2007
$2.3M
Mechanism of Actin mRNA LocalizationR01GM084364 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SINGER, ROBERT H · 2008 to 2012
$1.9M
NIAMS NIH HHS AR41480NIAMS NIH HHS R01 AR041480NIGMS NIH HHS GM84364NIGMS NIH HHS R01 GM084364
6 · The paper itself

Abstract

In primary neurons, the oncofetal RNA-binding protein IGF2BP1 (IGF2 mRNA-binding protein 1) controls spatially restricted β-actin (ACTB) mRNA translation and modulates growth cone guidance. In cultured tumor-derived cells, IGF2BP1 was shown to regulate the formation of lamellipodia and invadopodia. However, how and via which target mRNAs IGF2BP1 controls the motility of tumor-derived cells has remained elusive. In this study, we reveal that IGF2BP1 promotes the velocity and directionality of tumor-derived cell migration by determining the cytoplasmic fate of two novel target mRNAs: MAPK4 and PTEN. Inhibition of MAPK4 mRNA translation by IGF2BP1 antagonizes MK5 activation and prevents phosphorylation of HSP27, which sequesters actin monomers available for F-actin polymerization. Consequently, HSP27-ACTB association is reduced, mobilizing cellular G-actin for polymerization in order to promote the velocity of cell migration. At the same time, stabilization of the PTEN mRNA by IGF2BP1 enhances PTEN expression and antagonizes PIP(3)-directed signaling. This enforces the directionality of cell migration in a RAC1-dependent manner by preventing additional lamellipodia from forming and sustaining cell polarization intrinsically. IGF2BP1 thus promotes the velocity and persistence of tumor cell migration by controlling the expression of signaling proteins. This fine-tunes and connects intracellular signaling networks in order to enhance actin dynamics and cell polarization.

Indexed as

Signal TransductionActinsCell Line, TumorCell MovementCell PolarityEnzyme ActivationExtracellular Signal-Regulated MAP KinasesHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHumansIntracellular Signaling Peptides and ProteinsMolecular ChaperonesPhosphorylationProtein Serine-Threonine KinasesPTEN PhosphohydrolaseRNA, MessengerActinsExtracellular Signal-Regulated MAP KinasesHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSPB1 protein, humanIntracellular Signaling Peptides and ProteinsMAP-kinase-activated kinase 5Molecular ChaperonesProtein Serine-Threonine KinasesPTEN PhosphohydrolasePTEN protein, humanRNA, Messenger

Identifiers

PMID22279049
PMCPMC3273841
OpenAlexW2168844797

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.