Evidence map›Paper›PMID 25772449›Full record

ArticleCurrent biology : CB2015

A dynamin-actin interaction is required for vesicle scission during endocytosis in yeast.

Sarah E Palmer, Iwona I Smaczynska-de Rooij, Christopher J Marklew, Ellen G Allwood, Ritu Mishra, Simeon Johnson, Martin W Goldberg, Kathryn R Ayscough

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Emerging Mechanisms of Endocytosis inLife (Basel, Switzerland) · 2021
    Review
  7. Frontiers in cell and developmental biology · 2021
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Mechanisms of clathrin-mediated endocytosis.Nature reviews. Molecular cell biology · 2018
    Review
  14. Article
  15. Article
  16. Dynamin Autonomously Regulates Podocyte Focal Adhesion Maturation.Journal of the American Society of Nephrology : JASN · 2017
    Article
  17. Article
  18. Article
  19. Review
  20. 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

8 authors at 2 institutions in 1 country.

Sarah E PalmerDepartment of Biomedical Science, University of Sheffield, Sheffield S10 2TN, UK.
Iwona I Smaczynska-de RooijDepartment of Biomedical Science, University of Sheffield, Sheffield S10 2TN, UK.
Christopher J MarklewDepartment of Biomedical Science, University of Sheffield, Sheffield S10 2TN, UK.
Ellen G AllwoodDepartment of Biomedical Science, University of Sheffield, Sheffield S10 2TN, UK.
Ritu MishraDepartment of Biological Science, Durham University, Durham DH1 3LE, UK.
Simeon JohnsonDepartment of Biological Science, Durham University, Durham DH1 3LE, UK.
Martin W GoldbergDepartment of Biological Science, Durham University, Durham DH1 3LE, UK.
Kathryn R AyscoughDepartment of Biomedical Science, University of Sheffield, Sheffield S10 2TN, UK. Electronic address: k.ayscough@sheffield.ac.uk.
University of Sheffield · GBDurham University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G011818/1Biotechnology and Biological Sciences Research Council BB/K002511/1Medical Research CouncilWellcome TrustWellcome Trust 093134MA
6 · The paper itself

Abstract

Actin is critical for endocytosis in yeast cells, and also in mammalian cells under tension. However, questions remain as to how force generated through actin polymerization is transmitted to the plasma membrane to drive invagination and scission. Here, we reveal that the yeast dynamin Vps1 binds and bundles filamentous actin. Mutational analysis of Vps1 in a helix of the stalk domain identifies a mutant RR457-458EE that binds actin more weakly. In vivo analysis of Vps1 function demonstrates that the mutation disrupts endocytosis but not other functions of Vps1 such as vacuolar trafficking or peroxisome fission. The mutant Vps1 is stably expressed in cells and co-localizes with the endocytic reporters Abp1 and the amphiphysin Rvs167. Detailed analysis of individual endocytic patch behavior indicates that the mutation causes aberrant movements in later stages of endocytosis, consistent with a scission defect. Ultrastructural analysis of yeast cells using electron microscopy reveals a significant increase in invagination depth, further supporting a role for the Vps1-actin interaction during scission. In vitro analysis of the mutant protein demonstrates that--like wild-type Vps1--it is able to form oligomeric rings, but, critically, it has lost its ability to bundle actin filaments into higher-order structures. A model is proposed in which actin filaments bind Vps1 during invagination, and this interaction is important to transduce the force of actin polymerization to the membrane to drive successful scission.

Indexed as

ActinsDynaminsEndocytosisGTP-Binding ProteinsMicrofilament ProteinsNerve Tissue ProteinsProtein TransportSaccharomyces cerevisiae ProteinsTransport VesiclesVesicular Transport ProteinsYeastsABP1 protein, S cerevisiaeActinsamphiphysinDynaminsGTP-Binding ProteinsMicrofilament ProteinsNerve Tissue ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsVPS1 protein, S cerevisiae

Identifiers

PMID25772449
PMCPMC4386032
OpenAlexW1970190717

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.