Evidence map›Paper›PMID 22505844›Full record

ArticlePLoS biology2012

A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis.

Marcus J Taylor, Marko Lampe, Christien J Merrifield

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

97 citing papers in PubMed, 147 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Review
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  7. Bend it like BIN1: how a membrane-curving adaptor protein shapes cardiac physiology.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Dynamin-dependent entry ofResearch square · 2023
    Article
  15. Generation of nanoscopic membrane curvature for membrane trafficking.Nature reviews. Molecular cell biology · 2023
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

37 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Marcus J TaylorMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Marko Lampe
Christien J Merrifield
MRC Laboratory of Molecular Biology · GBLaboratoire d'Enzymologie et Biochimie Structurales · FR

Funding

Medical Research Council MC_U105178789Medical Research Council U105178789
6 · The paper itself

Abstract

Clathrin-mediated endocytosis proceeds by a sequential series of reactions catalyzed by discrete sets of protein machinery. The final reaction in clathrin-mediated endocytosis is membrane scission, which is mediated by the large guanosine triophosphate hydrolase (GTPase) dynamin and which may involve the actin-dependent recruitment of N-terminal containing BIN/Amphiphysin/RVS domain containing (N-BAR) proteins. Optical microscopy has revealed a detailed picture of when and where particular protein types are recruited in the ∼20-30 s preceding scission. Nevertheless, the regulatory mechanisms and functions that underpin protein recruitment are not well understood. Here we used an optical assay to investigate the coordination and interdependencies between the recruitment of dynamin, the actin cytoskeleton, and N-BAR proteins to individual clathrin-mediated endocytic scission events. These measurements revealed that a feedback loop exists between dynamin and actin at sites of membrane scission. The kinetics of dynamin, actin, and N-BAR protein recruitment were modulated by dynamin GTPase activity. Conversely, acute ablation of actin dynamics using latrunculin-B led to a ∼50% decrease in the incidence of scission, an ∼50% decrease in the amplitude of dynamin recruitment, and abolished actin and N-BAR recruitment to scission events. Collectively these data suggest that dynamin, actin, and N-BAR proteins work cooperatively to efficiently catalyze membrane scission. Dynamin controls its own recruitment to scission events by modulating the kinetics of actin and N-BAR recruitment to sites of scission. Conversely actin serves as a dynamic scaffold that concentrates dynamin and N-BAR proteins at sites of scission.

Indexed as

EndocytosisFeedback, PhysiologicalActinsAnimalsBridged Bicyclo Compounds, HeterocyclicCell MembraneClathrinClathrin-Coated VesiclesCytoskeletal ProteinsDynamin IKineticsMiceMutation, MissenseNIH 3T3 CellsProtein Serine-Threonine KinasesProtein TransportActinsBridged Bicyclo Compounds, HeterocyclicClathrinCytoskeletal ProteinsDynamin IGAK protein, mouselatrunculin BProtein Serine-Threonine KinasesRecombinant Fusion ProteinsThiazolidines

Identifiers

PMID22505844
PMCPMC3323523
OpenAlexW2068177704

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.