| Acidification of the lysosome-like vacuole and the vacuolar H+-ATPase are deficient in two yeast mutants that fail to sort vacuolar proteins. | |
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MedLine Citation:
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PMID: 2526133 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Organelle acidification plays a demonstrable role in intracellular protein processing, transport, and sorting in animal cells. We investigated the relationship between acidification and protein sorting in yeast by treating yeast cells with ammonium chloride and found that this lysosomotropic agent caused the mislocalization of a substantial fraction of the newly synthesized vacuolar (lysosomal) enzyme proteinase A (PrA) to the cell surface. We have also determined that a subset of the vpl mutants, which are deficient in sorting of vacuolar proteins (Rothman, J. H., and T. H. Stevens. 1986. Cell. 47:1041-1051; Rothman, J. H., I. Howald, and T. H. Stevens. EMBO [Eur. Mol. Biol. Organ.] J. In press), failed to accumulate the lysosomotropic fluorescent dye quinacrine within their vacuoles, mimicking the phenotype of wild-type cells treated with ammonium. The acidification defect of vpl3 and vpl6 mutants correlated with a marked deficiency in vacuolar ATPase activity, diminished levels of two immunoreactive subunits of the protontranslocating ATPase (H+-ATPase) in purified vacuolar membranes, and accumulation of the intracellular portion of PrA as the precursor species. Therefore, some of the VPL genes are required for the normal function of the yeast vacuolar H+-ATPase complex and may encode either subunits of the enzyme or components required for its assembly and targeting. Collectively, these findings implicate a critical role for acidification in vacuolar protein sorting and zymogen activation in yeast, and suggest that components of the yeast vacuolar acidification system may be identified by examining mutants defective in sorting of vacuolar proteins. |
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Authors:
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J H Rothman; C T Yamashiro; C K Raymond; P M Kane; T H Stevens |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of cell biology Volume: 109 ISSN: 0021-9525 ISO Abbreviation: J. Cell Biol. Publication Date: 1989 Jul |
Date Detail:
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Created Date: 1989-08-21 Completed Date: 1989-08-21 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 0375356 Medline TA: J Cell Biol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 93-100 Citation Subset: IM |
Affiliation:
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Institute of Molecular Biology, University of Oregon, Eugene 97403. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphatases
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genetics,
metabolism* Blotting, Western Cell Compartmentation* Fungal Proteins / metabolism* Hydrogen-Ion Concentration* Lysosomes / drug effects, metabolism* Mutation Quinacrine / metabolism, pharmacology Saccharomyces cerevisiae / genetics Vacuoles / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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PHS 32448/PH/PHPPO CDC HHS |
| Chemical | |
Reg. No./Substance:
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0/Fungal Proteins; 83-89-6/Quinacrine; EC 3.6.1.-/Adenosine Triphosphatases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
| Full Text | |
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Journal Information Journal ID (nlm-ta): J Cell Biol ISSN: 0021-9525 ISSN: 1540-8140 Publisher: The Rockefeller University Press |
Article Information Download PDF  Print publication date: Day: 1 Month: 7 Year: 1989 Volume: 109 Issue: 1 First Page: 93 Last Page: 100 ID: 2115461 Publisher Id: 89308889 PubMed Id: 2526133 |
| Acidification of the lysosome-like vacuole and the vacuolar H+-ATPase are deficient in two yeast mutants that fail to sort vacuolar proteins | |
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