Evidence map›Paper›PMID 25775509›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Endocytic proteins drive vesicle growth via instability in high membrane tension environment.

Nikhil Walani, Jennifer Torres, Ashutosh Agrawal

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Vesiculation pathways in clathrin-mediated endocytosis.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Biophysical modeling of membrane curvature generation and curvature sensing by the glycocalyx.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Value of models for membrane budding.Current opinion in cell biology · 2021
    Review
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Nikhil WalaniDepartment of Mechanical Engineering, University of Houston, Houston, TX 77204.
Jennifer TorresDepartment of Mechanical Engineering, University of Houston, Houston, TX 77204.
Ashutosh AgrawalDepartment of Mechanical Engineering, University of Houston, Houston, TX 77204 ashutosh@uh.edu.
University of Houston · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clathrin-mediated endocytosis (CME) is a key pathway for transporting cargo into cells via membrane vesicles; it plays an integral role in nutrient import, signal transduction, neurotransmission, and cellular entry of pathogens and drug-carrying nanoparticles. Because CME entails substantial local remodeling of the plasma membrane, the presence of membrane tension offers resistance to bending and hence, vesicle formation. Experiments show that in such high-tension conditions, actin dynamics is required to carry out CME successfully. In this study, we build on these pioneering experimental studies to provide fundamental mechanistic insights into the roles of two key endocytic proteins-namely, actin and BAR proteins-in driving vesicle formation in high membrane tension environment. Our study reveals an actin force-induced "snap-through instability" that triggers a rapid shape transition from a shallow invagination to a highly invaginated tubular structure. We show that the association of BAR proteins stabilizes vesicles and induces a milder instability. In addition, we present a rather counterintuitive role of BAR depolymerization in regulating the shape evolution of vesicles. We show that the dissociation of BAR proteins, supported by actin-BAR synergy, leads to considerable elongation and squeezing of vesicles. Going beyond the membrane geometry, we put forth a stress-based perspective for the onset of vesicle scission and predict the shapes and composition of detached vesicles. We present the snap-through transition and the high in-plane stress as possible explanations for the intriguing direct transformation of broad and shallow invaginations into detached vesicles in BAR mutant yeast cells.

Indexed as

EndocytosisActin CytoskeletonActinsAnimalsBiological TransportCarrier ProteinsCell MembraneClathrinClathrin-Coated VesiclesDogsMacromolecular SubstancesMadin Darby Canine Kidney CellsMembrane LipidsMembrane ProteinsModels, TheoreticalPolymersActinsCarrier ProteinsClathrinMacromolecular SubstancesMembrane LipidsMembrane ProteinsPolymersactinBAR proteinsclathrin-mediated endocytosisinstabilitymembrane tension

Identifiers

PMID25775509
PMCPMC4378438
OpenAlexW2042749721

What OpenQuestion holds

Textmetadata
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.