Journal article
Yeast Vps45p is a Sec1p-like protein required for the consumption of vacuole-targeted, post-Golgi transport vesicles
European journal of cell biology, Vol.65(2), pp.305-318
12/01/1994
PMID: 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.
Details
- Title: Subtitle
- Yeast Vps45p is a Sec1p-like protein required for the consumption of vacuole-targeted, post-Golgi transport vesicles
- Creators
- R C PiperE A WhittersT H Stevens
- Resource Type
- Journal article
- Publication Details
- European journal of cell biology, Vol.65(2), pp.305-318
- PMID
- 7720726
- ISSN
- 0171-9335
- eISSN
- 1618-1298
- Language
- English
- Date published
- 12/01/1994
- Academic Unit
- Molecular Physiology and Biophysics; Medicine Administration; Internal Medicine
- Record Identifier
- 9984297606502771
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