The ESCRTs - converging on mechanism
The endosomal sorting complexes required for transport (ESCRTs) I, -II and -III, and their associated factors are a collection of ∼20 proteins in yeast and ∼30 in mammals, responsible for severing membrane necks in processes that range from multivesicular body formation, HIV release and cytokinesis,...
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creator | Remec Pavlin, Mark Hurley, James H |
description | The endosomal sorting complexes required for transport (ESCRTs) I, -II and -III, and their associated factors are a collection of ∼20 proteins in yeast and ∼30 in mammals, responsible for severing membrane necks in processes that range from multivesicular body formation, HIV release and cytokinesis, to plasma and lysosomal membrane repair. ESCRTs are best known for 'reverse-topology' membrane scission, where they act on the inner surface of membrane necks, often when membranes are budded away from the cytosol. These events are driven by membrane-associated assemblies of dozens to hundreds of ESCRT molecules. ESCRT-III proteins form filaments with a variety of geometries and ESCRT-I has now been shown to also form helical structures. The complex nature of the system and the unusual topology of its action has made progress challenging, and led to controversies with regard to its underlying mechanism. This Review will focus on recent advances obtained by structural
reconstitution and
mechanistic studies, and places them in their biological context. The field is converging towards a consensus on the broad outlines of a mechanism that is driven by a progressive ATP-dependent treadmilling exchange of ESCRT subunits, as well as compositional change and geometric transitions in ESCRT filaments. |
doi_str_mv | 10.1242/jcs.240333 |
format | Article |
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reconstitution and
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reconstitution and
mechanistic studies, and places them in their biological context. The field is converging towards a consensus on the broad outlines of a mechanism that is driven by a progressive ATP-dependent treadmilling exchange of ESCRT subunits, as well as compositional change and geometric transitions in ESCRT filaments.</description><subject>Review</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNpVkEtLAzEUhYMotlY3_gCZhQsRpuY1yWQjSKkPKAha1-FOJtNOmUlqMi347x1pLbq6i_txzuFD6JLgMaGc3q1MHFOOGWNHaEi4lKkiTB6jIcaUpCpjbIDOYlxhjCVV8hQNGFUsF7kaouv50ibT98nbPCZpYrzb2rCo3SLxLmmtWYKrY3uOTipoor3Y3xH6eJzOJ8_p7PXpZfIwSw3nvEtLkisruWWQAeWE0koIZWglOYOyqMBARXA_M5dAykKCICAzzkwOYIQoSjZC97vc9aZobWms6wI0eh3qFsKX9lDr_x9XL_XCb7XMKOZ91Ajd7AOC_9zY2Om2jsY2DTjrN1FTzvt2JSTp0dsdaoKPMdjqUEOw_tGqe616p7WHr_4OO6C_Htk3PP5yPw</recordid><startdate>20200916</startdate><enddate>20200916</enddate><creator>Remec Pavlin, Mark</creator><creator>Hurley, James H</creator><general>The Company of Biologists Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-5054-5445</orcidid></search><sort><creationdate>20200916</creationdate><title>The ESCRTs - converging on mechanism</title><author>Remec Pavlin, Mark ; Hurley, James H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c444t-d189e74e3a5a24122f669c2f743adbfacaf1003387a1db7a61a7543c8aac66bd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Review</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Remec Pavlin, Mark</creatorcontrib><creatorcontrib>Hurley, James H</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Remec Pavlin, Mark</au><au>Hurley, James H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The ESCRTs - converging on mechanism</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2020-09-16</date><risdate>2020</risdate><volume>133</volume><issue>18</issue><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>The endosomal sorting complexes required for transport (ESCRTs) I, -II and -III, and their associated factors are a collection of ∼20 proteins in yeast and ∼30 in mammals, responsible for severing membrane necks in processes that range from multivesicular body formation, HIV release and cytokinesis, to plasma and lysosomal membrane repair. ESCRTs are best known for 'reverse-topology' membrane scission, where they act on the inner surface of membrane necks, often when membranes are budded away from the cytosol. These events are driven by membrane-associated assemblies of dozens to hundreds of ESCRT molecules. ESCRT-III proteins form filaments with a variety of geometries and ESCRT-I has now been shown to also form helical structures. The complex nature of the system and the unusual topology of its action has made progress challenging, and led to controversies with regard to its underlying mechanism. This Review will focus on recent advances obtained by structural
reconstitution and
mechanistic studies, and places them in their biological context. The field is converging towards a consensus on the broad outlines of a mechanism that is driven by a progressive ATP-dependent treadmilling exchange of ESCRT subunits, as well as compositional change and geometric transitions in ESCRT filaments.</abstract><cop>England</cop><pub>The Company of Biologists Ltd</pub><pmid>32938689</pmid><doi>10.1242/jcs.240333</doi><orcidid>https://orcid.org/0000-0001-5054-5445</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Review |
title | The ESCRTs - converging on mechanism |
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