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Design principles of the ESCRT-III Vps24-Vps2 module
ESCRT-III polymerization is required for all endosomal sorting complex required for transport (ESCRT)-dependent events in the cell. However, the relative contributions of the eight ESCRT-III subunits differ between each process. The minimal features of ESCRT-III proteins necessary for function and t...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8143795/ https://www.ncbi.nlm.nih.gov/pubmed/34028356 http://dx.doi.org/10.7554/eLife.67709 |
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author | Banjade, Sudeep Shah, Yousuf H Tang, Shaogeng Emr, Scott D |
author_facet | Banjade, Sudeep Shah, Yousuf H Tang, Shaogeng Emr, Scott D |
author_sort | Banjade, Sudeep |
collection | PubMed |
description | ESCRT-III polymerization is required for all endosomal sorting complex required for transport (ESCRT)-dependent events in the cell. However, the relative contributions of the eight ESCRT-III subunits differ between each process. The minimal features of ESCRT-III proteins necessary for function and the role for the multiple ESCRT-III subunits remain unclear. To identify essential features of ESCRT-III subunits, we previously studied the polymerization mechanisms of two ESCRT-III subunits Snf7 and Vps24, identifying the association of the helix-4 region of Snf7 with the helix-1 region of Vps24 (Banjade et al., 2019a). Here, we find that mutations in the helix-1 region of another ESCRT-III subunit Vps2 can functionally replace Vps24 in Saccharomyces cerevisiae. Engineering and genetic selections revealed the required features of both subunits. Our data allow us to propose three minimal features required for ESCRT-III function – spiral formation, lateral association of the spirals through heteropolymerization, and binding to the AAA + ATPase Vps4 for dynamic remodeling. |
format | Online Article Text |
id | pubmed-8143795 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-81437952021-05-26 Design principles of the ESCRT-III Vps24-Vps2 module Banjade, Sudeep Shah, Yousuf H Tang, Shaogeng Emr, Scott D eLife Biochemistry and Chemical Biology ESCRT-III polymerization is required for all endosomal sorting complex required for transport (ESCRT)-dependent events in the cell. However, the relative contributions of the eight ESCRT-III subunits differ between each process. The minimal features of ESCRT-III proteins necessary for function and the role for the multiple ESCRT-III subunits remain unclear. To identify essential features of ESCRT-III subunits, we previously studied the polymerization mechanisms of two ESCRT-III subunits Snf7 and Vps24, identifying the association of the helix-4 region of Snf7 with the helix-1 region of Vps24 (Banjade et al., 2019a). Here, we find that mutations in the helix-1 region of another ESCRT-III subunit Vps2 can functionally replace Vps24 in Saccharomyces cerevisiae. Engineering and genetic selections revealed the required features of both subunits. Our data allow us to propose three minimal features required for ESCRT-III function – spiral formation, lateral association of the spirals through heteropolymerization, and binding to the AAA + ATPase Vps4 for dynamic remodeling. eLife Sciences Publications, Ltd 2021-05-24 /pmc/articles/PMC8143795/ /pubmed/34028356 http://dx.doi.org/10.7554/eLife.67709 Text en © 2021, Banjade 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 | Biochemistry and Chemical Biology Banjade, Sudeep Shah, Yousuf H Tang, Shaogeng Emr, Scott D Design principles of the ESCRT-III Vps24-Vps2 module |
title | Design principles of the ESCRT-III Vps24-Vps2 module |
title_full | Design principles of the ESCRT-III Vps24-Vps2 module |
title_fullStr | Design principles of the ESCRT-III Vps24-Vps2 module |
title_full_unstemmed | Design principles of the ESCRT-III Vps24-Vps2 module |
title_short | Design principles of the ESCRT-III Vps24-Vps2 module |
title_sort | design principles of the escrt-iii vps24-vps2 module |
topic | Biochemistry and Chemical Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8143795/ https://www.ncbi.nlm.nih.gov/pubmed/34028356 http://dx.doi.org/10.7554/eLife.67709 |
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