Abstract
The ESCRT-I and ESCRT-II complexes help sort ubiquitinated proteins into vesicles that accumulate within multivesicular bodies (MVBs). Crystallographic and biochemical analyses reveal that the GLUE domain of the human ESCRT-II EAP45 (also called VPS36) subunit is a split pleckstrin-homology domain that binds ubiquitin along one edge of the beta-sandwich. The structure suggests how human ESCRT-II can couple recognition of ubiquitinated cargoes and endosomal phospholipids during MVB protein sorting.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Motifs
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Binding Sites
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism*
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Crystallography, X-Ray
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Endosomal Sorting Complexes Required for Transport
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Endosomes / metabolism
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Humans
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Models, Molecular
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Molecular Sequence Data
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Protein Folding
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Protein Structure, Tertiary
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Protein Transport
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Transport Vesicles / metabolism*
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Ubiquitin / chemistry
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Ubiquitin / metabolism*
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Vesicular Transport Proteins / chemistry
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Vesicular Transport Proteins / metabolism
Substances
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Carrier Proteins
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Endosomal Sorting Complexes Required for Transport
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Recombinant Fusion Proteins
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Ubiquitin
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VPS36 protein, human
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Vesicular Transport Proteins