Evidence map›Paper›PMID 30504247›Full record

ArticleThe Journal of cell biology2019

BAR scaffolds drive membrane fission by crowding disordered domains.

Wilton T Snead, Wade F Zeno, Grace Kago, Ryan W Perkins, J Blair Richter, Chi Zhao, Eileen M Lafer, Jeanne C Stachowiak

Abstract readComparative StudyVideo-Audio Media
In one paragraph

Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
–field-weighted citation impact
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

48 citing papers in PubMed.

  1. Article
  2. Devising a divisome for synthetic cells.Nature reviews. Chemistry · 2026
    Review
  3. The disordered and structured regions ofbioRxiv : the preprint server for biology · 2026
    Article
  4. Clathrin is an Intrinsic Driver of Membrane Fission.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
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  17. Article
  18. Article
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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.

Wilton T SneadDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX.ORCID 0000-0003-1411-1281
Wade F ZenoDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX.
Grace KagoDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX.
Ryan W PerkinsDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX.
J Blair RichterDepartment of Biochemistry and Structural Biology, Center for Biomedical Neuroscience, University of Texas Health Science Center at San Antonio, San Antonio, TX.
Chi ZhaoDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX.
Eileen M LaferDepartment of Biochemistry and Structural Biology, Center for Biomedical Neuroscience, University of Texas Health Science Center at San Antonio, San Antonio, TX.
Jeanne C StachowiakDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX jcstach@austin.utexas.edu.ORCID 0000-0003-2501-142X

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Robin Jean Leach · 1991 to 2026
$59.1M
Protein Networks as Synergistic Drivers of Membrane TrafficR01GM112065 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI STACHOWIAK, JEANNE CASSTEVENS · 2014 to 2020
$2.5M
Elucidating the physical mechanisms of membrane fissionF31GM121013 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI SNEAD, WILTON THOMAS · 2016 to 2017
$71k
NCI NIH HHS P30 CA054174NIGMS NIH HHS F31 GM121013NIGMS NIH HHS R01 GM112065
6 · The paper itself

Abstract

Cellular membranes are continuously remodeled. The crescent-shaped bin-amphiphysin-rvs (BAR) domains remodel membranes in multiple cellular pathways. Based on studies of isolated BAR domains in vitro, the current paradigm is that BAR domain-containing proteins polymerize into cylindrical scaffolds that stabilize lipid tubules. But in nature, proteins that contain BAR domains often also contain large intrinsically disordered regions. Using in vitro and live cell assays, here we show that full-length BAR domain-containing proteins, rather than stabilizing membrane tubules, are instead surprisingly potent drivers of membrane fission. Specifically, when BAR scaffolds assemble at membrane surfaces, their bulky disordered domains become crowded, generating steric pressure that destabilizes lipid tubules. More broadly, we observe this behavior with BAR domains that have a range of curvatures. These data suggest that the ability to concentrate disordered domains is a key driver of membrane remodeling and fission by BAR domain-containing proteins.

Indexed as

Adaptor Proteins, Vesicular TransportAnimalsCaenorhabditis elegans ProteinsCell LineCell MembraneHumansIntrinsically Disordered ProteinsLipid BilayersModels, MolecularMonomeric Clathrin Assembly ProteinsNerve Tissue ProteinsProtein DomainsRatsStructure-Activity RelationshipAdaptor Proteins, Vesicular TransportamphiphysinBAIAP2 protein, humanCaenorhabditis elegans Proteinsclathrin assembly protein AP180epsinIntrinsically Disordered ProteinsLipid BilayersMonomeric Clathrin Assembly ProteinsNerve Tissue Proteins

Identifiers

PMID30504247
PMCPMC6363457

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.