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Interplay of self-organization of microtubule asters and crosslinking protein condensates
The cytoskeleton is a major focus of physical studies to understand organization inside cells given its primary role in cell motility, cell division, and cell mechanics. Recently, protein condensation has been shown to be another major intracellular organizational strategy. Here, we report that the...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10367440/ https://www.ncbi.nlm.nih.gov/pubmed/37497046 http://dx.doi.org/10.1093/pnasnexus/pgad231 |
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author | Sahu, Sumon Chauhan, Prashali Lumen, Ellie Moody, Kelsey Peddireddy, Karthik Mani, Nandini Subramanian, Radhika Robertson-Anderson, Rae Wolfe, Aaron J Ross, Jennifer L |
author_facet | Sahu, Sumon Chauhan, Prashali Lumen, Ellie Moody, Kelsey Peddireddy, Karthik Mani, Nandini Subramanian, Radhika Robertson-Anderson, Rae Wolfe, Aaron J Ross, Jennifer L |
author_sort | Sahu, Sumon |
collection | PubMed |
description | The cytoskeleton is a major focus of physical studies to understand organization inside cells given its primary role in cell motility, cell division, and cell mechanics. Recently, protein condensation has been shown to be another major intracellular organizational strategy. Here, we report that the microtubule crosslinking proteins, MAP65-1 and PRC1, can form phase separated condensates at physiological salt and temperature without additional crowding agents in vitro. The size of the droplets depends on the concentration of protein. MAP65 condensates are liquid at first and can gelate over time. We show that these condensates can nucleate and grow microtubule bundles that form asters, regardless of the viscoelasticity of the condensate. The droplet size directly controls the number of projections in the microtubule asters, demonstrating that the MAP65 concentration can control the organization of microtubules. When gel-like droplets nucleate and grow asters from a shell of tubulin at the surface, the microtubules are able to re-fluidize the MAP65 condensate, returning the MAP65 molecules to solution. This work implies that there is an interplay between condensate formation from microtubule-associated proteins, microtubule organization, and condensate dissolution that could be important for the dynamics of intracellular organization. |
format | Online Article Text |
id | pubmed-10367440 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-103674402023-07-26 Interplay of self-organization of microtubule asters and crosslinking protein condensates Sahu, Sumon Chauhan, Prashali Lumen, Ellie Moody, Kelsey Peddireddy, Karthik Mani, Nandini Subramanian, Radhika Robertson-Anderson, Rae Wolfe, Aaron J Ross, Jennifer L PNAS Nexus Physical Sciences and Engineering The cytoskeleton is a major focus of physical studies to understand organization inside cells given its primary role in cell motility, cell division, and cell mechanics. Recently, protein condensation has been shown to be another major intracellular organizational strategy. Here, we report that the microtubule crosslinking proteins, MAP65-1 and PRC1, can form phase separated condensates at physiological salt and temperature without additional crowding agents in vitro. The size of the droplets depends on the concentration of protein. MAP65 condensates are liquid at first and can gelate over time. We show that these condensates can nucleate and grow microtubule bundles that form asters, regardless of the viscoelasticity of the condensate. The droplet size directly controls the number of projections in the microtubule asters, demonstrating that the MAP65 concentration can control the organization of microtubules. When gel-like droplets nucleate and grow asters from a shell of tubulin at the surface, the microtubules are able to re-fluidize the MAP65 condensate, returning the MAP65 molecules to solution. This work implies that there is an interplay between condensate formation from microtubule-associated proteins, microtubule organization, and condensate dissolution that could be important for the dynamics of intracellular organization. Oxford University Press 2023-07-13 /pmc/articles/PMC10367440/ /pubmed/37497046 http://dx.doi.org/10.1093/pnasnexus/pgad231 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of National Academy of Sciences. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Physical Sciences and Engineering Sahu, Sumon Chauhan, Prashali Lumen, Ellie Moody, Kelsey Peddireddy, Karthik Mani, Nandini Subramanian, Radhika Robertson-Anderson, Rae Wolfe, Aaron J Ross, Jennifer L Interplay of self-organization of microtubule asters and crosslinking protein condensates |
title | Interplay of self-organization of microtubule asters and crosslinking protein condensates |
title_full | Interplay of self-organization of microtubule asters and crosslinking protein condensates |
title_fullStr | Interplay of self-organization of microtubule asters and crosslinking protein condensates |
title_full_unstemmed | Interplay of self-organization of microtubule asters and crosslinking protein condensates |
title_short | Interplay of self-organization of microtubule asters and crosslinking protein condensates |
title_sort | interplay of self-organization of microtubule asters and crosslinking protein condensates |
topic | Physical Sciences and Engineering |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10367440/ https://www.ncbi.nlm.nih.gov/pubmed/37497046 http://dx.doi.org/10.1093/pnasnexus/pgad231 |
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