Evidence map›Paper›PMID 24959909›Full record

ArticlePloS one2014

A new role for myosin II in vesicle fission.

Juan A Flores, Santiago Balseiro-Gomez, Jose M Cabeza, Jorge Acosta, Pilar Ramirez-Ponce, Eva Ales

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

6 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. An acto-myosin II constricting ring initiates the fission of activity-dependent bulk endosomes in neurosecretory cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    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

6 authors at 1 institution in 1 country.

Juan A FloresDpto. Fisiología Médica y Biofísica, Facultad de Medicina, Universidad de Sevilla, Seville, Spain.
Santiago Balseiro-GomezDpto. Fisiología Médica y Biofísica, Facultad de Medicina, Universidad de Sevilla, Seville, Spain.
Jose M CabezaDpto. Fisiología Médica y Biofísica, Facultad de Medicina, Universidad de Sevilla, Seville, Spain.
Jorge AcostaDpto. Fisiología Médica y Biofísica, Facultad de Medicina, Universidad de Sevilla, Seville, Spain.
Pilar Ramirez-PonceDpto. Fisiología Médica y Biofísica, Facultad de Medicina, Universidad de Sevilla, Seville, Spain.
Eva AlesDpto. Fisiología Médica y Biofísica, Facultad de Medicina, Universidad de Sevilla, Seville, Spain.
Universidad de Sevilla · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An endocytic vesicle is formed from a flat plasma membrane patch by a sequential process of invagination, bud formation and fission. The scission step requires the formation of a tubular membrane neck (the fission pore) that connects the endocytic vesicle with the plasma membrane. Progress in vesicle fission can be measured by the formation and closure of the fission pore. Live-cell imaging and sensitive biophysical measurements have provided various glimpses into the structure and behaviour of the fission pore. In the present study, the role of non-muscle myosin II (NM-2) in vesicle fission was tested by analyzing the kinetics of the fission pore with perforated-patch clamp capacitance measurements to detect single vesicle endocytosis with millisecond time resolution in peritoneal mast cells. Blebbistatin, a specific inhibitor of NM-2, dramatically increased the duration of the fission pore and also prevented closure during large endocytic events. Using the fluorescent markers FM1-43 and pHrodo Green dextran, we found that NM-2 inhibition greatly arrested vesicle fission in a late phase of the scission event when the pore reached a final diameter of ∼ 5 nm. Our results indicate that loss of the ATPase activity of myosin II drastically reduces the efficiency of membrane scission by making vesicle closure incomplete and suggest that NM-2 might be especially relevant in vesicle fission during compound endocytosis.

Indexed as

AnimalsCell MembraneEndocytosisExocytosisHeterocyclic Compounds, 4 or More RingsMast CellsMiceMyosin Type IIProtein BindingPyridinium CompoundsQuaternary Ammonium CompoundsTransport VesiclesblebbistatinFM1 43Heterocyclic Compounds, 4 or More RingsMyosin Type IIPyridinium CompoundsQuaternary Ammonium Compounds

Identifiers

PMID24959909
PMCPMC4069105
OpenAlexW2040360409

What OpenQuestion holds

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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.