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PMID: 1493335 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants.

Molecular biology of the cell ·Vol. 3 ·No. 12 ·1992-12-00 ·Pages 1389-402

Raymond CK, Howald-Stevenson I, Vater CA, Stevens TH

Abstract

The collection of vacuolar protein sorting mutants (vps mutants) in Saccharomyces cerevisiae comprises of 41 complementation groups. The vacuoles in these mutant strains were examined using immunofluorescence microscopy. Most of the vps mutants were found to possess vacuolar morphologies that differed significantly from wild-type vacuoles. Furthermore, mutants representing independent vps complementation groups were found to share aberrant morphological features. Six distinct classes of vacuolar morphology were observed. Mutants from eight vps complementation groups were defective both for vacuolar segregation from mother cells into developing buds and for acidification of the vacuole. Another group of mutants, represented by 13 complementation groups, accumulated a novel organelle distinct from the vacuole that contained a late-Golgi protein, active vacuolar H(+)-ATPase complex, and soluble vacuolar hydrolases. We suggest that this organelle may represent an exaggerated endosome-like compartment. None of the vps mutants appeared to mislocalize significant amounts of the vacuolar membrane protein alkaline phosphatase. Quantitative immunoprecipitations of the soluble vacuolar hydrolase carboxypeptidase Y (CPY) were performed to determine the extent of the sorting defect in each vps mutant. A good correlation between morphological phenotype and the extent of the CPY sorting defect was observed.

Related Genes
vps vpt
MeSH Terms
Carboxypeptidases/metabolism Cathepsin A Fungal Proteins/metabolism Genetic Complementation Test Genotype Mutation Protein Processing, Post-Translational Proton-Translocating ATPases/metabolism Saccharomyces cerevisiae/genetics,metabolism,ultrastructure Saccharomyces cerevisiae Proteins Vacuoles/metabolism,ultrastructure
Chemicals
Fungal Proteins Saccharomyces cerevisiae Proteins Carboxypeptidases Cathepsin A PRC1 protein, S cerevisiae serine carboxypeptidase Proton-Translocating ATPases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Raymond C K
Institute of Molecular Biology, University of Oregon, Eugene 97403.
Howald-Stevenson I
Vater C A
Stevens T H
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
DOI
10.1091/mbc.3.12.1389
Published
1992-12-00
Pages
1389-402
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC275707
Subset
IM
Grants
NIGMS NIH HHS · GM-32448 · United States
Corrections
CommentIn
PMID: 22798387
External Links
PubMed source DOI: 10.1091/mbc.3.12.1389 PMC Full Text View journal details
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