Evidence map›Paper›PMID 31951196›Full record

ArticleeLife2020

Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis.

Matthew Akamatsu, Ritvik Vasan, Daniel Serwas, Michael A Ferrin, Padmini Rangamani, David G Drubin

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
13.3field-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

96 citing papers in PubMed, 162 citations in OpenAlex.

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36 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

6 authors at 2 institutions in 1 country.

Matthew AkamatsuDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.ORCID 0000-0002-0286-5310
Ritvik VasanDepartment of Mechanical and Aerospace Engineering, University of California, San Diego, La Jolla, United States.
Daniel SerwasDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.ORCID 0000-0001-9010-7298
Michael A FerrinDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.ORCID 0000-0002-9899-1169
Padmini RangamaniDepartment of Mechanical and Aerospace Engineering, University of California, San Diego, La Jolla, United States.ORCID 0000-0001-5953-4347
David G DrubinDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.ORCID 0000-0003-3002-6271
University of California, Berkeley · USUniversity of California San Diego · 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
Molecular and biophysical mechanism of plasma membrane internalization during nonclathrin endocytosisK99GM132551 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI AKAMATSU, MATTHEW SATARO · 2019 to 2020
$194k
Army Research Office W911NF1610411Human Frontier Science Program LT000234/2018-LNIGMS NIH HHS K99 GM132551NIGMS NIH HHS R35 GM118149Office of Naval Research N00014-17-1-2628
6 · The paper itself

Abstract

Force generation by actin assembly shapes cellular membranes. An experimentally constrained multiscale model shows that a minimal branched actin network is sufficient to internalize endocytic pits against membrane tension. Around 200 activated Arp2/3 complexes are required for robust internalization. A newly developed molecule-counting method determined that ~200 Arp2/3 complexes assemble at sites of clathrin-mediated endocytosis in human cells. Simulations predict that actin self-organizes into a radial branched array with growing ends oriented toward the base of the pit. Long actin filaments bend between attachment sites in the coat and the base of the pit. Elastic energy stored in bent filaments, whose presence was confirmed by cryo-electron tomography, contributes to endocytic internalization. Elevated membrane tension directs more growing filaments toward the base of the pit, increasing actin nucleation and bending for increased force production. Thus, spatially constrained actin filament assembly utilizes an adaptive mechanism enabling endocytosis under varying physical constraints.

Indexed as

Actin CytoskeletonActinsCell MembraneClathrinActin-Related Protein 2-3 ComplexBiomechanical PhenomenaCell LineEndocytosisHumansInduced Pluripotent Stem CellsActin-Related Protein 2-3 ComplexActinsClathrinactin mechanicscell biologyclathrin-mediated endocytosiscryo-electron tomographyhumanhuman induced pluripotent stem cellsmultiscale modelingphysics of living systemsquantitative microscopy

Identifiers

PMID31951196
PMCPMC7041948
OpenAlexW2999931938

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.