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Vps60 initiates alternative ESCRT-III filaments

Endosomal sorting complex required for transport-III (ESCRT-III) participates in essential cellular functions, from cell division to endosome maturation. The remarkable increase of its subunit diversity through evolution may have enabled the acquisition of novel functions. Here, we characterize a no...

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Autores principales: Pfitzner, Anna-Katharina, Zivkovic, Henry, Bernat-Silvestre, César, West, Matt, Peltier, Tanner, Humbert, Frédéric, Odorizzi, Greg, Roux, Aurélien
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10538557/
https://www.ncbi.nlm.nih.gov/pubmed/37768378
http://dx.doi.org/10.1083/jcb.202206028
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author Pfitzner, Anna-Katharina
Zivkovic, Henry
Bernat-Silvestre, César
West, Matt
Peltier, Tanner
Humbert, Frédéric
Odorizzi, Greg
Roux, Aurélien
author_facet Pfitzner, Anna-Katharina
Zivkovic, Henry
Bernat-Silvestre, César
West, Matt
Peltier, Tanner
Humbert, Frédéric
Odorizzi, Greg
Roux, Aurélien
author_sort Pfitzner, Anna-Katharina
collection PubMed
description Endosomal sorting complex required for transport-III (ESCRT-III) participates in essential cellular functions, from cell division to endosome maturation. The remarkable increase of its subunit diversity through evolution may have enabled the acquisition of novel functions. Here, we characterize a novel ESCRT-III copolymer initiated by Vps60. Membrane-bound Vps60 polymers recruit Vps2, Vps24, Did2, and Ist1, as previously shown for Snf7. Snf7- and Vps60-based filaments can coexist on membranes without interacting as their polymerization and recruitment of downstream subunits remain spatially and biochemically separated. In fibroblasts, Vps60/CHMP5 and Snf7/CHMP4 are both recruited during endosomal functions and cytokinesis, but their localization is segregated and their recruitment dynamics are different. Contrary to Snf7/CHMP4, Vps60/CHMP5 is not recruited during nuclear envelope reformation. Taken together, our results show that Vps60 and Snf7 form functionally distinct ESCRT-III polymers, supporting the notion that diversification of ESCRT-III subunits through evolution is linked to the acquisition of new cellular functions.
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spelling pubmed-105385572023-09-29 Vps60 initiates alternative ESCRT-III filaments Pfitzner, Anna-Katharina Zivkovic, Henry Bernat-Silvestre, César West, Matt Peltier, Tanner Humbert, Frédéric Odorizzi, Greg Roux, Aurélien J Cell Biol Article Endosomal sorting complex required for transport-III (ESCRT-III) participates in essential cellular functions, from cell division to endosome maturation. The remarkable increase of its subunit diversity through evolution may have enabled the acquisition of novel functions. Here, we characterize a novel ESCRT-III copolymer initiated by Vps60. Membrane-bound Vps60 polymers recruit Vps2, Vps24, Did2, and Ist1, as previously shown for Snf7. Snf7- and Vps60-based filaments can coexist on membranes without interacting as their polymerization and recruitment of downstream subunits remain spatially and biochemically separated. In fibroblasts, Vps60/CHMP5 and Snf7/CHMP4 are both recruited during endosomal functions and cytokinesis, but their localization is segregated and their recruitment dynamics are different. Contrary to Snf7/CHMP4, Vps60/CHMP5 is not recruited during nuclear envelope reformation. Taken together, our results show that Vps60 and Snf7 form functionally distinct ESCRT-III polymers, supporting the notion that diversification of ESCRT-III subunits through evolution is linked to the acquisition of new cellular functions. Rockefeller University Press 2023-09-28 /pmc/articles/PMC10538557/ /pubmed/37768378 http://dx.doi.org/10.1083/jcb.202206028 Text en © 2023 Pfitzner et al. https://creativecommons.org/licenses/by/4.0/This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Pfitzner, Anna-Katharina
Zivkovic, Henry
Bernat-Silvestre, César
West, Matt
Peltier, Tanner
Humbert, Frédéric
Odorizzi, Greg
Roux, Aurélien
Vps60 initiates alternative ESCRT-III filaments
title Vps60 initiates alternative ESCRT-III filaments
title_full Vps60 initiates alternative ESCRT-III filaments
title_fullStr Vps60 initiates alternative ESCRT-III filaments
title_full_unstemmed Vps60 initiates alternative ESCRT-III filaments
title_short Vps60 initiates alternative ESCRT-III filaments
title_sort vps60 initiates alternative escrt-iii filaments
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10538557/
https://www.ncbi.nlm.nih.gov/pubmed/37768378
http://dx.doi.org/10.1083/jcb.202206028
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