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Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis
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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7041948/ https://www.ncbi.nlm.nih.gov/pubmed/31951196 http://dx.doi.org/10.7554/eLife.49840 |
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author | Akamatsu, Matthew Vasan, Ritvik Serwas, Daniel Ferrin, Michael A Rangamani, Padmini Drubin, David G |
author_facet | Akamatsu, Matthew Vasan, Ritvik Serwas, Daniel Ferrin, Michael A Rangamani, Padmini Drubin, David G |
author_sort | Akamatsu, Matthew |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7041948 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-70419482020-02-27 Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis Akamatsu, Matthew Vasan, Ritvik Serwas, Daniel Ferrin, Michael A Rangamani, Padmini Drubin, David G eLife Cell Biology 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. eLife Sciences Publications, Ltd 2020-01-17 /pmc/articles/PMC7041948/ /pubmed/31951196 http://dx.doi.org/10.7554/eLife.49840 Text en © 2020, Akamatsu et al https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Cell Biology Akamatsu, Matthew Vasan, Ritvik Serwas, Daniel Ferrin, Michael A Rangamani, Padmini Drubin, David G Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis |
title | Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis |
title_full | Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis |
title_fullStr | Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis |
title_full_unstemmed | Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis |
title_short | Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis |
title_sort | principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7041948/ https://www.ncbi.nlm.nih.gov/pubmed/31951196 http://dx.doi.org/10.7554/eLife.49840 |
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