Evidence map›Paper›PMID 27502487›Full record

ArticleThe Journal of cell biology2016

ERK signaling promotes cell motility by inducing the localization of myosin 1E to lamellipodial tips.

Susumu Tanimura, Junya Hashizume, Naoya Arichika, Kazushi Watanabe, Kaname Ohyama, Kohsuke Takeda, Michiaki Kohno

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. LSP1-myosin1e bimolecular complex regulates focal adhesion dynamics and cell migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  10. The Emerging Roles of π Subunit-Containing GABAInternational journal of medical sciences · 2021
    Review
  11. ERK signalling: a master regulator of cell behaviour, life and fate.Nature reviews. Molecular cell biology · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. ERK Activity Imaging During Migration of Living Cells In Vitro and In Vivo.International journal of molecular sciences · 2019
    Review
  16. Article
  17. Article
  18. Review
  19. Osteoclast stimulation factor 1 (Ostf1) KNOCKOUT increases trabecular bone mass in mice.Mammalian genome : official journal of the International Mammalian Genome Society · 2017
    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

7 authors at 1 institution in 1 country.

Susumu TanimuraDepartment of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan Nagasaki University Research Centre for Genomic Instability and Carcinogenesis, Nagasaki 852-8523, Japan tani1211@nagasaki-u.ac.jp kohnom@nagasaki-u.ac.jp.
Junya HashizumeDepartment of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
Naoya ArichikaDepartment of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
Kazushi WatanabeDepartment of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
Kaname OhyamaDepartment of Pharmacy Practice, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan Nagasaki University Research Centre for Genomic Instability and Carcinogenesis, Nagasaki 852-8523, Japan.
Kohsuke TakedaDepartment of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
Michiaki KohnoDepartment of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan tani1211@nagasaki-u.ac.jp kohnom@nagasaki-u.ac.jp.ORCID 0000-0002-7644-0059
Nagasaki University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signaling by extracellular signal-regulated kinase (ERK) plays an essential role in the induction of cell motility, but the precise mechanism underlying such regulation has remained elusive. We recently identified SH3P2 as a negative regulator of cell motility whose function is inhibited by p90 ribosomal S6 kinase (RSK)-mediated phosphorylation downstream of ERK. We here show that myosin 1E (Myo1E) is a binding partner of SH3P2 and that the interaction of the two proteins in the cytosol prevents the localization of Myo1E to the plasma membrane. Serum-induced phosphorylation of SH3P2 at Ser(202) by RSK results in dissociation of Myo1E from SH3P2 in the cytosol and the subsequent localization of Myo1E to the tips of lamellipodia mediated by binding of its TH2 domain to F-actin. This translocation of Myo1E is essential for lamellipodium extension and consequent cell migration. The ERK signaling pathway thus promotes cell motility through regulation of the subcellular localization of Myo1E.

Indexed as

Cell MovementMAP Kinase Signaling SystemAmino Acid SequenceCell Line, TumorHumansIntracellular Signaling Peptides and ProteinsModels, BiologicalMyosin Type IPhosphorylationPhosphoserineProlineProtein BindingProtein DomainsProteinsProtein TransportPseudopodiaIntracellular Signaling Peptides and ProteinsMYO1E protein, humanMyosin Type IOSTF1 protein, humanPhosphoserineProlineProteinsRibosomal Protein S6 Kinases, 90-kDa

Identifiers

PMID27502487
PMCPMC4987290
OpenAlexW2495580168

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.