Evidence map›Paper›PMID 24337113›Full record

ArticleBiology open2013

Myosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation.

Prabuddha Gupta, Nils C Gauthier, Yu Cheng-Han, Yuan Zuanning, Bruno Pontes, Malte Ohmstede, René Martin, Hans-Joachim Knölker, Hans-Günther Döbereiner, Mira Krendel and 1 more

Open access · goldAbstract read
In one paragraph

Article in Biology open, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Unconventional Myosins fromBiomolecules · 2022
    Review
  8. Article
  9. Review
  10. 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
  11. Myosin 1b is an actin depolymerase.Nature communications · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Myosin-I molecular motors at a glance.Journal of cell science · 2016
    Review
  18. Article
  19. 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

11 authors at 4 institutions in 3 countries.

Prabuddha GuptaMechanobiology Institute, National University of Singapore, Singapore 117411.
Nils C Gauthier
Yu Cheng-Han
Yuan Zuanning
Bruno Pontes
Malte Ohmstede
René Martin
Hans-Joachim Knölker
Hans-Günther Döbereiner
Mira Krendel
Michael Sheetz
National University of Singapore · SGTU Dresden · DEUniversity of Bremen · DESUNY Upstate Medical University · US

Funding

Role of myosin 1e in podocyte biology and renal filtrationR01DK083345 · NIDDK · UPSTATE MEDICAL UNIVERSITY · PI Mira Krendel · 2011 to 2026
$6.8M
NIDDK NIH HHS R01 DK083345
6 · The paper itself

Abstract

Because the actin network in active lamellipodia is continuously assembling at the edge, moving inward and disassembling, there is a question as to how actin-binding proteins and other components are transported to the leading edge and how nascent adhesions are stabilized. Active transport could play a significant role in these functions but the components involved are unknown. We show here that Myosin 1E (a long tailed Myosin 1 isoform) rapidly moves to the tips of active lamellipodia and to actin-rich early adhesions, unlike Myosin 1G, 1B or 1C (short tailed isoforms). Myosin 1E co-localizes with CARMIL, FHOD1, Arp3 and β3-integrin in those early adhesions. But these structures precede stable paxillin-rich adhesions. Myosin 1E movement depends upon actin-binding domains and the presence of an SH3 oligomerization domain. Overexpression of a Myosin 1E deletion mutant without the extreme C-terminal interacting (SH3) domain (Myosin 1EΔSH3) increases edge fluctuations and decreases stable adhesion lifetimes. In contrast, overexpression of Myosin 1E full tail domain (TH1+TH2+TH3/SH3) decreases edge fluctuation. In Myosin 1E knockdown cells, and more prominently in cells treated with Myosin 1 inhibitor, cell-matrix adhesions are also short-lived and fail to mature. We suggest that, by moving to actin polymerization sites and early adhesion sites in active lamellipodia, Myosin 1E might play important roles in transporting not only important polymerizing proteins but also proteins involved in adhesion stabilization.

Indexed as

Cell–matrix adhesionMyosin 1ETransport

Identifiers

PMID24337113
PMCPMC3863413
OpenAlexW2103773342

What OpenQuestion 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 OpenQuestion graph.