Vacuolar ATPase mutants accumulate precursor proteins in a pre-vacuolar compartment

Debbie S. Yaver, Hannah Nelson, Nathan Nelson, Daniel J. Klionsky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

The vacuole of the yeast Saccharomyces cerevisiae contains a proton-translocating ATPase that acidifies the vacuolar lumen and generates an electrochemical potential across the vacuole membrane. Strains with chromosomal disruptions of the genes encoding the A, B, and c subunits of the vacuolar ATPase accumulate precursor forms of the vacuolar membrane protein alkaline phosphatase, and the soluble vacuolar hydrolases carboxypeptidase Y and proteinase A. We have found that the intracellular precursors in Δvat strains accumulate within the secretory pathway at some point before delivery to the vacuole but after transit to the Golgi complex. Purified vacuoles from Δvat cells do not contain the precursor forms of carboxypeptidase Y or alkaline phosphatase. In addition, vacuolar hydrolase-invertase hybrid proteins are inefficiently delivered to the vacuole in Δvat strains as demonstrated by vacuole isolation. Further subcellular fractionation to separate organelles indicate that significant amounts of the carboxypeptidase Y-invertase and alkaline phosphatase-invertase hybrid proteins are located in the late Golgi complex and/or post Golgi compartments.

Original languageEnglish
Pages (from-to)10564-10572
Number of pages9
JournalJournal of Biological Chemistry
Volume268
Issue number14
StatePublished - 15 May 1993
Externally publishedYes

Funding

FundersFunder number
National Institute of Diabetes and Digestive and Kidney DiseasesR01DK043684

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