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      Assembly and disassembly of the ESCRT-III membrane scission complex

      review-article
      Author(s): a , a , *
      Publication date PMC-release:
      Journal: Febs Letters
      Publisher: Elsevier Science B.V
      Keywords: ESCRT, Vps4, Multivesicular body (MVB), HIV, Cytokinesis

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          Highlights

          ► Three different ESCRT pathways activate ESCRT-III on distinct target membranes. ► Assembly of ESCRT-III filaments on membranes. ► Vps4 mediated disassembly of ESCRT-III and its role in MVB vesicle formation.

          Abstract

          The ESCRT (endosomal sorting complex required for transport) pathway promotes the final membrane scission step at the end of cytokinesis, assists viral budding and generates multivesicular bodies (MVBs). These seemingly unrelated processes require a topologically similar membrane deformation and scission event that buds membranes/vesicles out of the cytoplasm. The topology of this budding reaction is ‘opposite’ to reactions that bud endocytic and secretory vesicles into the cytoplasm. Here we summarize recent findings that help to understand how the ESCRT machinery, in particular the ESCRT-III complex, assembles on its target membranes, executes membrane scission and is disassembled by the AAA-ATPase Vps4.

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          Molecular Mechanism of Multivesicular Body Biogenesis by ESCRT Complexes

          Thomas Wollert, James Hurley (2010)
          When internalized receptors and other cargo are destined for lysosomal degradation, they are ubiquitinated and sorted by the ESCRT complexes 0, I, II, and III into multivesicular bodies. Multivesicular bodies are formed when cargo-rich patches of the limiting membrane of endosomes bud inward by an unknown mechanism and are then cleaved to yield cargo-bearing intralumenal vesicles. The biogenesis of multivesicular bodies was reconstituted and visualized using giant unilamellar vesicles, fluorescent ESCRT-0, I, II, and III complexes, and a membrane-tethered fluorescent ubiquitin fusion as a model cargo. ESCRT-0 forms domains of clustered cargo but does not deform membranes. ESCRT-I and II in combination deform the membrane into buds, in which cargo is confined. ESCRT-I and II localize to the bud necks, and recruit ESCRT-0-ubiquitin domains to the buds. ESCRT-III subunits localize to the bud neck and efficiently cleave the buds to form intralumenal vesicles. Intralumenal vesicles produced in this reaction contain the model cargo but are devoid of ESCRTs. The observations explain how the ESCRTs direct membrane budding and scission from the cytoplasmic side of the bud without being consumed in the reaction.
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            Membrane scission by the ESCRT-III complex.

            Thomas Wollert, Christian Wunder, Jennifer Lippincott-Schwartz … (2009)
            The endosomal sorting complex required for transport (ESCRT) system is essential for multivesicular body biogenesis, in which cargo sorting is coupled to the invagination and scission of intralumenal vesicles. The ESCRTs are also needed for budding of enveloped viruses including human immunodeficiency virus 1, and for membrane abscission in cytokinesis. In Saccharomyces cerevisiae, ESCRT-III consists of Vps20, Snf7, Vps24 and Vps2 (also known as Did4), which assemble in that order and require the ATPase Vps4 for their disassembly. In this study, the ESCRT-III-dependent budding and scission of intralumenal vesicles into giant unilamellar vesicles was reconstituted and visualized by fluorescence microscopy. Here we show that three subunits of ESCRT-III, Vps20, Snf7 and Vps24, are sufficient to detach intralumenal vesicles. Vps2, the ESCRT-III subunit responsible for recruiting Vps4, and the ATPase activity of Vps4 were required for ESCRT-III recycling and supported additional rounds of budding. The minimum set of ESCRT-III and Vps4 proteins capable of multiple cycles of vesicle detachment corresponds to the ancient set of ESCRT proteins conserved from archaea to animals.
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              Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting.

              Markus Babst, David Katzmann, Eden Estepa-Sabal … (2002)
              The sorting of transmembrane proteins (e.g., cell surface receptors) into the multivesicular body (MVB) pathway to the lysosomal/vacuolar lumen requires the function of the ESCRT protein complexes. The soluble coiled-coil-containing proteins Vps2, Vps20, Vps24, and Snf7 are recruited from the cytoplasm to endosomal membranes where they oligomerize into a protein complex, ESCRT-III. ESCRT-III contains two functionally distinct subcomplexes. The Vps20-Snf7 subcomplex binds to the endosomal membrane, in part via the myristoyl group of Vps20. The Vps2-Vps24 subcomplex binds to the Vps20-Snf7 complex and thereby serves to recruit additional cofactors to this site of protein sorting. We provide evidence for a role for ESCRT-III in sorting and/or concentration of MVB cargoes.
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                Author and article information

                Journal
                Journal ID (nlm-ta): FEBS Lett
                Journal ID (iso-abbrev): FEBS Lett
                Title: Febs Letters
                Publisher: Elsevier Science B.V
                ISSN (Print): 0014-5793
                ISSN (Electronic): 1873-3468
                Publication date PMC-release: 20 October 2011
                Publication date (Print): 20 October 2011
                Volume: 585
                Issue: 20
                Pages: 3191-3196
                Affiliations
                [a ]Division Cell Biology, Medical University Innsbruck, Innsbruck 6020, Austria
                Author notes
                [* ]Corresponding author. Fax: +43 512900373100. david.teis@ 123456i-med.ac.at
                Article
                Publisher ID: FEBS34920
                DOI: 10.1016/j.febslet.2011.09.001
                PMC ID: 3192940
                PubMed ID: 21924267
                SO-VID: 1cf90fa4-157b-492a-b1cf-8a6b8fb9244b
                Copyright © © 2011 Elsevier B.V.
                License:

                This document may be redistributed and reused, subject to certain conditions.

                History
                Date received : 3 August 2011
                Date revision received : 27 August 2011
                Date accepted : 4 September 2011
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: multivesicular body (mvb),vps4,hiv,escrt,cytokinesis
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: multivesicular body (mvb), vps4, hiv, escrt, cytokinesis

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