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- W96091585 abstract "The Endosomal Sorting Complexes Required for Transport (ESCRTs) comprise a highly conserved set of five protein complexes that function as a ubiquitin-dependent protein sorting machine which recognizes and directs the down-regulation of membrane proteins including signaling receptors. Recent studies have identified the ESCRT-III complex as a vesicle budding machine that can sort cargo into intraluminal vesicles (ILV) which bud into an endosomal multi-vesicular body (MVB). The mechanisms by which soluble ESCRT-III subunits (Vps20, Snf7, Vps24 and Vps2) mediate ILV budding are not yet known. Here, we present data indicating that conformational changes within the ESCRT-III subunit Snf7 (displacement of helix-5) activate Snf7 for membrane binding. Using electron microscopy techniques, we directly visualize ESCRT-III assembly on lipid monolayers. Activated Snf7 generates long ~9nm-wide protofilaments composed of two ~4nm sub-filaments. These protofilaments form 2-D spiral arrays on the monolayers. Strikingly, the addition of Vps24 and Vps2 transforms the flat spirals into 3-D membranesculpting helices. Finally, addition of ESCRT-II stabilizes the formation of ESCRT-III rings that are ~65 nm in diameter. We will discuss the role of domains in ESCRT-III subunits that function in cargo capture, membrane binding/deformation and scission during intraluminal vesicle formation." @default.
- W96091585 created "2016-06-24" @default.
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- W96091585 date "2013-04-01" @default.
- W96091585 modified "2023-10-18" @default.
- W96091585 title "ESCRTing Receptor Down‐Regulation: Assembly and Function of the ESCRT‐III Complex" @default.
- W96091585 doi "https://doi.org/10.1096/fasebj.27.1_supplement.212.2" @default.
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