Journal
STRUCTURE
Volume 16, Issue 9, Pages 1345-1356Publisher
CELL PRESS
DOI: 10.1016/j.str.2008.06.010
Keywords
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Funding
- NIH [P41 RR-01081]
- Trinity College, Cambridge, and the Medical Research Council
- EMBO fellowship [ALTF 165-2007]
- NIH
- Medical Research Council
- MRC [MC_U105184319, MC_U105184308] Funding Source: UKRI
- Medical Research Council [MC_U105184308, MC_U105184319] Funding Source: researchfish
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The ESCRT machinery mediates sorting of ubiquitinated transmembrane proteins to lysosomes via multivesicular bodies (MVBs) and also has roles in cytokinesis and viral budding. The ESCRT-III subunits are metastable monomers that transiently assemble on membranes. However, the nature of these assemblies is unknown. Among the core yeast ESCRT-III subunits, Snf7 and Vps24 spontaneously form ordered polymers in vitro. Single-particle EM reconstruction of helical Vps24 filaments shows both parallel and head-to-head subunit arrangements. Mutations of regions involved in intermolecular assembly in vitro result in cargo-sorting defects in vivo, suggesting that these homopolymers mimic interactions formed by ESCRT-III heteropolymers during MVB biogenesis. The C terminus of Vps24 is at the surface of the filaments and is not required for filament assembly. When this region is replaced by the MIT-interacting motif from the Vps2 subunit of ESCRT-III, the AAA-ATPase Vps4 can both bundle and disassemble the chimeric filaments in a nucleotide-dependent fashion.
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