Evidence map›Paper›PMID 22718763›Full record

ArticleThe Journal of biological chemistry2012

Nonmuscle myosin II is required for internalization of the epidermal growth factor receptor and modulation of downstream signaling.

Jong Hyun Kim, Aibing Wang, Mary Anne Conti, Robert S Adelstein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Kindlin-1 Regulates Epidermal Growth Factor Receptor Signaling.The Journal of investigative dermatology · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Small-molecule inhibitors of myosin proteins.Future medicinal chemistry · 2013
    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

4 authors at 2 institutions in 1 country.

Jong Hyun KimLaboratory of Molecular Cardiology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA. nr.kimjohn@gmail.com
Aibing Wang
Mary Anne Conti
Robert S Adelstein
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Light Microscopy CoreZICHL006019 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI COMBS, CHRISTIAN · 2009 to 2025
$29.3M
In Vivo Function of Nonmuscle Myosin II-AZIAHL004218 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ADELSTEIN, ROBERT · 2009 to 2019
$5.1M
Studying Pentalogy of Cantrell in Humans and MiceZIAHL004230 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ADELSTEIN, ROBERT · 2009 to 2019
$4.5M
The Functions and Properties of Nonmuscle Myosin Heavy Chains ZIAHL004216 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ADELSTEIN, ROBERT · 2009 to 2014
$2.2M
Intramural NIH HHS Z99 HL999999
6 · The paper itself

Abstract

Ligand-induced internalization of the epidermal growth factor receptor (EGFR) is an important process for regulating signal transduction, cellular dynamics, and cell-cell communication. Here, we demonstrate that nonmuscle myosin II (NM II) is required for the internalization of the EGFR and to trigger the EGFR-dependent activation of ERK and AKT. The EGFR was identified as a protein that interacts with NM II by co-immunoprecipitation and mass spectrometry analysis. This interaction requires both the regulatory light chain 20 (RLC20) of NM II and the kinase domain of the EGFR. Two paralogs of NM II, NM II-A, and NM II-B can act to internalize the EGFR, depending on the cell type and paralog content of the cell line. Loss (siRNA) or inhibition (25 μm blebbistatin) of NM II attenuates the internalization of the EGFR and impairs EGFR-dependent activation of ERK and AKT. Both internalization of the EGFR and downstream signaling to ERK and AKT can be partially restored in siRNA-treated cells by introduction of wild type (WT) GFP-NM II, but cannot be restored by motor mutant NM II. Taken together, these results suggest that NM II plays a role in the internalization of the EGFR and EGFR-mediated signaling pathways.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsEnzyme ActivationErbB ReceptorsExtracellular Signal-Regulated MAP KinasesHEK293 CellsHumansMass SpectrometryNonmuscle Myosin Type IIANonmuscle Myosin Type IIBProtein TransportProto-Oncogene Proteins c-aktSignal TransductionEGFR protein, humanErbB ReceptorsExtracellular Signal-Regulated MAP KinasesNonmuscle Myosin Type IIANonmuscle Myosin Type IIBProto-Oncogene Proteins c-akt

Identifiers

PMID22718763
PMCPMC3431632
OpenAlexW2039304427

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.