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Mechanisms of ESCRT‐mediated cargo sorting and degradation
Author(s) -
Audhya Anjon,
Schuh Amber,
Mayers Jonathan,
Fyfe Ian,
Edwardson Michael
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.463.1
Subject(s) - escrt , endosome , endocytic cycle , microbiology and biotechnology , endomembrane system , ubiquitin , biogenesis , transport protein , chemistry , tsg101 , transmembrane protein , vesicle , biology , biochemistry , membrane , endocytosis , microvesicles , microrna , receptor , gene , cell , intracellular
Vesicle‐mediated cargo transport within the endomembrane system requires precise coordination between adaptor molecules, which recognize sorting signals on substrates, and factors that promote changes in membrane architecture. At endosomal compartments, a set of protein complexes collectively known as the ESCRT machinery sequesters transmembrane cargoes that harbor a ubiquitin modification and packages them into vesicles that bud into the endosome lumen. Using atomic force microscopy, we define the architecture of each ESCRT complex in the presence of physiologically relevant lipid bilayers. This analysis indicates that ESCRT‐0, ESCRT‐I, and ESCRT‐II function as heterotetrameric complexes that collectively bind and sequester ubiquitin‐modified cargoes. Additionally, our analysis reveals a mechanism by which ESCRT‐III membrane scission activity is both spatially and temporally regulated during multivesicular endosome biogenesis. A revised model describing ESCRT function during protein sorting in the endocytic pathway will be presented.