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-Structure paper
Title | Structure and assembly of ESCRT-III helical Vps24 filaments. |
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Journal, issue, pages | Sci Adv, Vol. 6, Issue 34, Page eaba4897, Year 2020 |
Publish date | Aug 19, 2020 |
Authors | Stefan T Huber / Siavash Mostafavi / Simon A Mortensen / Carsten Sachse / |
PubMed Abstract | ESCRT-III proteins mediate a range of cellular membrane remodeling activities such as multivesicular body biogenesis, cytokinesis, and viral release. Critical to these processes is the assembly of ...ESCRT-III proteins mediate a range of cellular membrane remodeling activities such as multivesicular body biogenesis, cytokinesis, and viral release. Critical to these processes is the assembly of ESCRT-III subunits into polymeric structures. In this study, we determined the cryo-EM structure of a helical assembly of Vps24 at 3.2-Å resolution and found that Vps24 adopts an elongated open conformation. Vps24 forms a domain-swapped dimer extended into protofilaments that associate into a double-stranded apolar filament. We demonstrate that, upon binding negatively charged lipids, Vps24 homopolymer filaments undergo partial disassembly into shorter filament fragments and oligomers. Upon the addition of Vps24, Vps2, and Snf7, liposomes are deformed into neck and tubular structures by an ESCRT-III heteropolymer coat. The filamentous Vps24 homopolymer assembly structure and interaction studies reveal how Vps24 could introduce unique geometric properties to mixed-type ESCRT-III heteropolymers and contribute to the process of membrane scission events. |
External links | Sci Adv / PubMed:32875105 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 3.2 Å |
Structure data | EMDB-11212, PDB-6zh3: |
Source |
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Keywords | LIPID BINDING PROTEIN / Filament / Helical / Membrane Remodeling |