The Vps27p–Hse1p complex binds ubiquitin and mediates endosomal protein sorting

Membrane proteins that are degraded in the vacuole of Saccharomyces cerevisiae are sorted into discrete intralumenal vesicles, analogous to the internal membranes of multi-vesiculated bodies (MVBs). Recently, it has shown that the attachment of ubiquitin (Ub) mediates sorting into lumenal membranes...

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Veröffentlicht in:	Nature cell biology 2002-07, Vol.4 (7), p.534-539
Hauptverfasser:	Bilodeau, Patricia S., Urbanowski, Jennifer L., Winistorfer, Stanley C., Piper, Robert C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Biomedical and Life Sciences brief-communication Cancer Research Carrier Proteins - genetics Carrier Proteins - metabolism Cell Biology Developmental Biology Endosomal Sorting Complexes Required for Transport Endosomes - metabolism Golgi Apparatus - metabolism Life Sciences Macromolecular Substances Membrane proteins Membrane Proteins - metabolism Membranes Molecular Sequence Data Mutation Physiological aspects Protein binding Protein-protein interactions Proteins Receptors, Cytoplasmic and Nuclear - genetics Receptors, Cytoplasmic and Nuclear - metabolism Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Stem Cells Ubiquitin - metabolism Vesicular Transport Proteins
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