Evidence map›Paper›PMID 31385806›Full record

ArticleeLife2019

Type-I myosins promote actin polymerization to drive membrane bending in endocytosis.

Hetty E Manenschijn, Andrea Picco, Markus Mund, Anne-Sophie Rivier-Cordey, Jonas Ries, Marko Kaksonen

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

  1. A local solution to local load: Myo1E as a tension-responsive actuator in clathrin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  6. A role for cross-linking proteins in actin filament network organization and force generation.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  15. Switch-2 determines MgFrontiers in physiology · 2024
    Article
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  18. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
    Article
  19. Self-organizing actin networks drive sequential endocytic protein recruitment and vesicle release on synthetic lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  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

6 authors at 2 institutions in 2 countries.

Hetty E ManenschijnDepartment of Biochemistry, University of Geneva, Geneva, Switzerland.ORCID 0000-0003-4957-0568
Andrea PiccoDepartment of Biochemistry, University of Geneva, Geneva, Switzerland.ORCID 0000-0003-2548-9183
Markus MundDepartment of Biochemistry, University of Geneva, Geneva, Switzerland.ORCID 0000-0001-6449-743X
Anne-Sophie Rivier-CordeyDepartment of Biochemistry, University of Geneva, Geneva, Switzerland.
Jonas RiesCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID 0000-0002-6640-9250
Marko KaksonenDepartment of Biochemistry, University of Geneva, Geneva, Switzerland.ORCID 0000-0003-3645-7689
University of Geneva · CHEuropean Molecular Biology Laboratory · DE

Funding

European Research Council ERC CoG-724489Swiss National Science Foundation 31003A_163267
6 · The paper itself

Abstract

Clathrin-mediated endocytosis in budding yeast requires the formation of a dynamic actin network that produces the force to invaginate the plasma membrane against the intracellular turgor pressure. The type-I myosins Myo3 and Myo5 are important for endocytic membrane reshaping, but mechanistic details of their function remain scarce. Here, we studied the function of Myo3 and Myo5 during endocytosis using quantitative live-cell imaging and genetic perturbations. We show that the type-I myosins promote, in a dose-dependent way, the growth and expansion of the actin network, which controls the speed of membrane and coat internalization. We found that this myosin-activity is independent of the actin nucleation promoting activity of myosins, and cannot be compensated for by increasing actin nucleation. Our results suggest a new mechanism for type-I myosins to produce force by promoting actin filament polymerization.

Indexed as

EndocytosisPolymerizationActinsCell MembraneIntravital MicroscopyMyosin Heavy ChainsMyosin Type ISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsMYO3 protein, S cerevisiaeMYO5 protein, S cerevisiaeMyosin Heavy ChainsMyosin Type ISaccharomyces cerevisiae Proteinsactincell biologyendocytosismyosinS. cerevisiae

Identifiers

PMID31385806
PMCPMC6684269
OpenAlexW2965963292

What OpenQuestion holds

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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.