Evidence map›Paper›PMID 36136763›Full record

ArticleJournal of the American Chemical Society2022

Removal of Stomatin, a Membrane-Associated Cell Division Protein, Results in Specific Cellular Lipid Changes.

Federico Donà, Cagakan Özbalci, Andrea Paquola, Federica Ferrentino, Stephen J Terry, Elisabeth M Storck, Gaoge Wang, Ulrike S Eggert

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 52% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 1 institution in 1 country.

Federico DonàRandall Centre for Cell and Molecular Biophysics, King's College London, London SE1 1UL, U.K.ORCID 0000-0002-4232-4762
Cagakan ÖzbalciRandall Centre for Cell and Molecular Biophysics, King's College London, London SE1 1UL, U.K.
Andrea PaquolaRandall Centre for Cell and Molecular Biophysics, King's College London, London SE1 1UL, U.K.
Federica FerrentinoRandall Centre for Cell and Molecular Biophysics, King's College London, London SE1 1UL, U.K.
Stephen J TerryRandall Centre for Cell and Molecular Biophysics, King's College London, London SE1 1UL, U.K.
Elisabeth M StorckRandall Centre for Cell and Molecular Biophysics, King's College London, London SE1 1UL, U.K.ORCID 0000-0003-0924-9913
Gaoge WangRandall Centre for Cell and Molecular Biophysics, King's College London, London SE1 1UL, U.K.
Ulrike S EggertRandall Centre for Cell and Molecular Biophysics, King's College London, London SE1 1UL, U.K.ORCID 0000-0003-0932-5525
King's College London · GB

Funding

Wellcome TrustWellcome Trust 110060/Z/15/Z
6 · The paper itself

Abstract

Lipids are key constituents of all cells, which express thousands of different lipid species. In most cases, it is not known why cells synthesize such diverse lipidomes, nor what regulates their metabolism. Although it is known that dividing cells specifically regulate their lipid content and that the correct lipid complement is required for successful division, it is unclear how lipids connect with the cell division machinery. Here, we report that the membrane protein stomatin is involved in the cytokinesis step of cell division. Although it is not a lipid biosynthetic enzyme, depletion of stomatin causes cells to change their lipidomes. These changes include specific lipid species, like ether lipids, and lipid families like phosphatidylcholines. Addition of exogenous phosphatidylcholines rescues stomatin-induced defects. These data suggest that stomatin interfaces with lipid metabolism. Stomatin has multiple contacts with the plasma membrane and we identify which sites are required for its role in cell division, as well as associated lipid shifts. We also show that stomatin's mobility on the plasma membrane changes during division, further supporting the requirement for a highly regulated physical interaction between membrane lipids and this newly identified cell division protein.

Indexed as

Lipid MetabolismMembrane ProteinsCell DivisionEthersMembrane LipidsPhosphatidylcholinesEthersMembrane LipidsMembrane ProteinsPhosphatidylcholines

Identifiers

PMID36136763
PMCPMC9545149
OpenAlexW4296691669

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.