[PDF][PDF] Membrane transport: ubiquitylation in endosomal sorting
S Dupré, C Volland, R Haguenauer-Tsapis - Current Biology, 2001 - cell.com
S Dupré, C Volland, R Haguenauer-Tsapis
Current Biology, 2001•cell.comIn yeast, membrane proteins from the biosynthetic and endocytic pathways must be
ubiquitylated for sorting to inward-budding vesicles in late endosomes, which give rise to
multivesicular bodies. A conserved protein complex containing the yeast Vps23p or its
mammalian counterpart Tsg101 may act as the ubiquitin receptor.
ubiquitylated for sorting to inward-budding vesicles in late endosomes, which give rise to
multivesicular bodies. A conserved protein complex containing the yeast Vps23p or its
mammalian counterpart Tsg101 may act as the ubiquitin receptor.
Abstract
In yeast, membrane proteins from the biosynthetic and endocytic pathways must be ubiquitylated for sorting to inward-budding vesicles in late endosomes, which give rise to multivesicular bodies. A conserved protein complex containing the yeast Vps23p or its mammalian counterpart Tsg101 may act as the ubiquitin receptor.
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