A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor

A number of the Saccharomyces cerevisiae vacuolar protein-sorting (vps) mutants exhibit an altered vacuolar morphology. Unlike wild-type cells that contain 1-3 large vacuolar structures, the class B vps5 and vps17 mutant cells contain 10-20 smaller vacuole-like compartments. To explore the role of t...

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Veröffentlicht in:	Molecular biology of the cell 1997-08, Vol.8 (8), p.1529-1541
Hauptverfasser:	Horazdovsky, B F, Davies, B A, Seaman, M N, McLaughlin, S A, Yoon, S, Emr, S D
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Carrier Proteins - genetics Carrier Proteins - isolation & purification ErbB Receptors - metabolism Fungal Proteins - metabolism Membrane Proteins - metabolism Molecular Sequence Data Receptors, Cell Surface - metabolism Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins Sequence Alignment Sequence Homology, Amino Acid Vacuoles - physiology Vesicular Transport Proteins
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