Abstract
The sorting of transmembrane proteins (e.g., cell surface receptors) into the multivesicular body (MVB) pathway to the lysosomal/vacuolar lumen requires the function of the ESCRT protein complexes. The soluble coiled-coil-containing proteins Vps2, Vps20, Vps24, and Snf7 are recruited from the cytoplasm to endosomal membranes where they oligomerize into a protein complex, ESCRT-III. ESCRT-III contains two functionally distinct subcomplexes. The Vps20-Snf7 subcomplex binds to the endosomal membrane, in part via the myristoyl group of Vps20. The Vps2-Vps24 subcomplex binds to the Vps20-Snf7 complex and thereby serves to recruit additional cofactors to this site of protein sorting. We provide evidence for a role for ESCRT-III in sorting and/or concentration of MVB cargoes.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Carrier Proteins / metabolism*
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Carrier Proteins / ultrastructure
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Cell Compartmentation / physiology*
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Cell Membrane / metabolism*
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Cell Membrane / ultrastructure
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Endosomal Sorting Complexes Required for Transport
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Endosomes / metabolism*
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Endosomes / ultrastructure
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Escherichia coli
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Eukaryotic Cells / metabolism*
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Eukaryotic Cells / ultrastructure
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Fungal Proteins / metabolism*
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Fungal Proteins / ultrastructure
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Lysosomes / metabolism
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Lysosomes / ultrastructure
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Macromolecular Substances
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Membrane Proteins / genetics
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Membrane Proteins / metabolism
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Microscopy, Electron
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Mutation / physiology
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Nuclear Proteins*
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Peptide Hydrolases / metabolism
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Protein Transport / physiology*
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Saccharomyces cerevisiae
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Saccharomyces cerevisiae Proteins*
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Transport Vesicles / metabolism*
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Transport Vesicles / ultrastructure
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trans-Golgi Network / metabolism
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trans-Golgi Network / ultrastructure
Substances
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Carrier Proteins
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Endosomal Sorting Complexes Required for Transport
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Fungal Proteins
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Macromolecular Substances
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Membrane Proteins
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Nuclear Proteins
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SNF7 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Peptide Hydrolases