Evidence map›Paper›PMID 30086165›Full record

ArticlePloS one2018

ATP competes with PIP2 for binding to gelsolin.

Dávid Szatmári, Bo Xue, Balakrishnan Kannan, Leslie D Burtnick, Beáta Bugyi, Miklós Nyitrai, Robert C Robinson

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Cytoskeleton-associated gelsolin responds to the midgut distention process in saline meal-fed Aedes aegypti and affects arbovirus dissemination from the midgut.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  6. Article
  7. The p53 and Calcium Regulated Actin Rearrangement in Model Cells.International journal of molecular sciences · 2022
    Article
  8. Article
  9. Review
  10. Review of PIP2 in Cellular Signaling, Functions and Diseases.International journal of molecular sciences · 2020
    Review
  11. Article
  12. Review
  13. Article
  14. 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 3 institutions in 4 countries.

Dávid SzatmáriInstitute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Singapore, Singapore.
Bo XueInstitute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Singapore, Singapore.ORCID 0000-0002-5172-2519
Balakrishnan KannanInstitute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Singapore, Singapore.
Leslie D BurtnickDepartment of Chemistry and Centre for Blood Research, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada.
Beáta BugyiUniversity of Pécs, Medical School, Department of Biophysics, Pécs, Hungary.
Miklós NyitraiUniversity of Pécs, Medical School, Department of Biophysics, Pécs, Hungary.
Robert C RobinsonInstitute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Singapore, Singapore.ORCID 0000-0001-6367-6903
Agency for Science, Technology and Research · SGUniversity of Pecs · HUUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gelsolin is a severing and capping protein that targets filamentous actin and regulates filament lengths near plasma membranes, contributing to cell movement and plasma membrane morphology. Gelsolin binds to the plasma membrane via phosphatidylinositol 4,5-bisphosphate (PIP2) in a state that cannot cap F-actin, and gelsolin-capped actin filaments are uncapped by PIP2 leading to filament elongation. The process by which gelsolin is removed from PIP2 at the plasma membrane is currently unknown. Gelsolin also binds ATP with unknown function. Here we characterize the role of ATP on PIP2-gelsolin complex dynamics. Fluorophore-labeled PIP2 and ATP were used to study their interactions with gelsolin using steady-state fluorescence anisotropy, and Alexa488-labeled gelsolin was utilized to reconstitute the regulation of gelsolin binding to PIP2-containing phospholipid vesicles by ATP. Under physiological salt conditions ATP competes with PIP2 for binding to gelsolin, while calcium causes the release of ATP from gelsolin. These data suggest a cycle for gelsolin activity. Firstly, calcium activates ATP-bound gelsolin allowing it to sever and cap F-actin. Secondly, PIP2-binding removes the gelsolin cap from F-actin at low calcium levels, leading to filament elongation. Finally, ATP competes with PIP2 to release the calcium-free ATP-bound gelsolin, allowing it to undergo a further round of severing.

Indexed as

ActinsAdenosine TriphosphateAnimalsBinding, CompetitiveCalciumCationsCell MembraneEscherichia coliGelsolinHumansKineticsMagnesiumPhosphatidylinositol 4,5-DiphosphatePolymerizationProtein BindingRabbitsActinsAdenosine TriphosphateCalciumCationsGelsolinMagnesiumPhosphatidylinositol 4,5-Diphosphate

Identifiers

PMID30086165
PMCPMC6080781
OpenAlexW2885409152

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.