Evidence map›Paper›PMID 23704935›Full record

ArticlePloS one2013

Dynamic regulation of extracellular signal-regulated kinase (ERK) by protein phosphatase 2A regulatory subunit B56γ1 in nuclei induces cell migration.

Ei Kawahara, Shiori Maenaka, Eri Shimada, Yoshihiro Nishimura, Hiroshi Sakurai

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Prognostic Impact of PPP2R5C Gene Expression in Adult Acute Myeloid Leukemia Patients with Normal Cytogenetics.Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion · 2020
    Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ei KawaharaDepartment of Clinical Laboratory Science, Kanazawa University, Kanazawa, Japan.
Shiori Maenaka
Eri Shimada
Yoshihiro Nishimura
Hiroshi Sakurai
Kanazawa University · JP

Funding

SYSTEMS CONNECTIVITY + BRAIN ACTIVATION:IMAGING STUDIES OF LANGUAGE + PERCEPTIONP50HD055748 · NICHD · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MINSHEW, NANCY J · 2007 to 2011
$9.7M
TRANS STUDIES OF COGNITIVE,AFFECTIVE/NEUROCHEMICAL PROCESSES UNDERLYING INSISTENCP50HD055751 · NICHD · UNIVERSITY OF ILLINOIS AT CHICAGO · PI OWLEY, THOMAS B · 2007 to 2011
$9.5M
Motor Control and Cerebellar Maturation in AutismK23MH092696 · NIMH · UT SOUTHWESTERN MEDICAL CENTER · PI MOSCONI, MATTHEW W · 2010 to 2014
$783k
NICHD NIH HHS HD055748NICHD NIH HHS HD055751NICHD NIH HHS HD35469NIMH NIH HHS MH092696
6 · The paper itself

Abstract

Extracellular signal-regulated kinase (ERK) signalling plays a central role in various biological processes, including cell migration, but it remains unknown what factors directly regulate the strength and duration of ERK activation. We found that, among the B56 family of protein phosphatase 2A (PP2A) regulatory subunits, B56γ1 suppressed EGF-induced cell migration on collagen, bound to phosphorylated-ERK, and dephosphorylated ERK, whereas B56α1 and B56β1 did not. B56γ1 was immunolocalized in nuclei. The IER3 protein was immediately highly expressed in response to costimulation of cells with EGF and collagen. Knockdown of IER3 inhibited cell migration and enhanced dephosphorylation of ERK. Analysis of the time course of PP2A-B56γ1 activity following the costimulation showed an immediate loss of phosphatase activity, followed by a rapid increase in activity, and this activity then remained at a stable level that was lower than the original level. Our results indicate that the strength and duration of the nuclear ERK activation signal that is initially induced by ERK kinase (MEK) are determined at least in part by modulation of the phosphatase activity of PP2A-B56γ1 through two independent pathways.

Indexed as

Cell Movement3T3 CellsAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsCell AdhesionCell NucleusCollagenEnzyme ActivationEpidermal Growth FactorExtracellular Signal-Regulated MAP KinasesHumansKineticsMembrane ProteinsMiceMitogen-Activated Protein Kinase KinasesApoptosis Regulatory ProteinsCollagenEpidermal Growth FactorExtracellular Signal-Regulated MAP KinasesIER3 protein, humanMembrane ProteinsMitogen-Activated Protein Kinase KinasesPpp2r5c protein, mouseProtein Phosphatase 2

Identifiers

PMID23704935
PMCPMC3660565
OpenAlexW2131375542

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.