Evidence map›Paper›PMID 1493335›Full record

ArticleMolecular biology of the cell1992

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

C K Raymond, I Howald-Stevenson, C A Vater, T H Stevens

Abstract read
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Article in Molecular biology of the cell, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 421 papers.

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0cells of the map it votes in
421citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

421 citing papers in PubMed.

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  7. Treatment ofFrontiers in toxicology · 2026
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  8. The V-ATPase VJournal of oral microbiology · 2026
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361 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

C K RaymondInstitute of Molecular Biology, University of Oregon, Eugene 97403.
I Howald-Stevenson
C A Vater
T H Stevens

Funding

Cell Biological Study of Eukaryotic Organelle AssemblyR37GM032448 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 2003 to 2012
$3.6M
CELL BIOLOGICAL STUDY OF EUKARYOTIC ORGANELLE ASSEMBLYR01GM032448 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 1985 to 2002
$970k
NIGMS NIH HHS GM-32448
6 · The paper itself

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.

Indexed as

MutationCarboxypeptidasesCathepsin AFungal ProteinsGenetic Complementation TestGenotypeProtein Processing, Post-TranslationalProton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesCarboxypeptidasesCathepsin AFungal ProteinsPRC1 protein, S cerevisiaeProton-Translocating ATPasesSaccharomyces cerevisiae Proteinsserine carboxypeptidase

Identifiers

PMID1493335
PMCPMC275707

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.