Yeast Vps45p is a Sec1p-like protein required for the consumption of vacuole-targeted, post-Golgi transport vesicles.
Eur J Cell Biol
; 65(2): 305-18, 1994 Dec.
Article
en En
| MEDLINE
| ID: mdl-7720726
ABSTRACT
Over 45 VPS genes (vacuolar protein sorting) in Saccharomyces cerevisiae are necessary for the correct sorting and delivery of vacuolar hydrolases. Yeast strains carrying mutations in a subset of these VPS genes (class D vps mutants) are also defective in the segregation of vacuolar material into the developing daughter cell and are morphologically characterized by having large central vacuoles. The class D VPS gene products, which include a Rab5 homologue (VPS21/YPT51) and a syntaxin homologue (PEP12/VPS6), have been proposed to function together at a particular step along the vacuolar protein sorting pathway. We have cloned another class D VPS gene, VPS45, which is homologous to a growing family of genes that encode Sec1p-like proteins. Vps45p is predicted to be a hydrophilic protein of 577 amino acids with a molecular mass of 67 kDa. Fractionation studies show that Vps45p is a peripheral membrane protein that cofractionates with Golgi-like membranes, consistent with Vps45p functioning in membrane traffic between the Golgi and the vacuole. Using a temperature-sensitive allele of VPS45, we show that inactivation of Vps45p causes the rapid accumulation of small (40-60 nm) vesicles and secretion of the vacuolar hydrolase carboxypeptidase Y. Because the entire yeast secretory pathway is functional after the temperature-induced inactivation of Vps45p, we conclude that the accumulated vesicles represent transport intermediates between the Golgi and the vacuole.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Vacuolas
/
Proteínas Fúngicas
/
Familia de Multigenes
/
Proteínas de Saccharomyces cerevisiae
/
Proteínas de Transporte Vesicular
/
Aparato de Golgi
/
Proteínas del Tejido Nervioso
Idioma:
En
Revista:
Eur J Cell Biol
Año:
1994
Tipo del documento:
Article