Evidence map›Paper›PMID 30659101›Full record

ArticleThe Journal of cell biology2019

Type I myosins anchor actin assembly to the plasma membrane during clathrin-mediated endocytosis.

Ross T A Pedersen, David G Drubin

Open access · bronzeAbstract readVideo-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 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.4field-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

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
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  6. Review
  7. 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
    Article
  8. Article
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  12. Article
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  15. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
    Article
  16. 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
  17. Article
  18. Article
  19. Article
  20. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    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

2 authors at 1 institution in 1 country.

Ross T A PedersenDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA.ORCID 0000-0002-3890-3972
David G DrubinDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA drubin@berkeley.edu.ORCID 0000-0003-3002-6271
University of California, Berkeley · US

Funding

Nikon confocal system for improved spatio-dynamic analysis of endocytic trafficking eventsR35GM118149 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DAVID G DRUBIN · 2016 to 2026
$12.0M
NIGMS NIH HHS R35 GM118149
6 · The paper itself

Abstract

The actin cytoskeleton generates forces on membranes for a wide range of cellular and subcellular morphogenic events, from cell migration to cytokinesis and membrane trafficking. For each of these processes, filamentous actin (F-actin) interacts with membranes and exerts force through its assembly, its associated myosin motors, or both. These two modes of force generation are well studied in isolation, but how they are coordinated in cells is mysterious. During clathrin-mediated endocytosis, F-actin assembly initiated by the Arp2/3 complex and several proteins that compose the WASP/myosin complex generates the force necessary to deform the plasma membrane into a pit. Here we present evidence that type I myosin is the key membrane anchor for endocytic actin assembly factors in budding yeast. By mooring actin assembly factors to the plasma membrane, this myosin organizes endocytic actin networks and couples actin-generated forces to the plasma membrane to drive invagination and scission. Through this unexpected mechanism, myosin facilitates force generation independent of its motor activity.

Indexed as

EndocytosisActin CytoskeletonActin-Related Protein 2-3 ComplexBinding SitesCell MembraneClathrinGene Expression Regulation, FungalMutationMyosin Type IProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionWiskott-Aldrich Syndrome ProteinActin-Related Protein 2-3 ComplexClathrinLAS17 protein, S cerevisiaeMYO5 protein, S cerevisiaeMyosin Type ISaccharomyces cerevisiae ProteinsWiskott-Aldrich Syndrome Protein

Identifiers

PMID30659101
PMCPMC6446854
OpenAlexW2909343602

What Socratic holds

Textmetadata
LicenceCC BY-NC-SA
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 Socratic graph.