Protein sorting in yeast: The localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide

We have isolated cis-acting mutations in the gene encoding the yeast vacuolar protein carboxypeptidase Y (CPY) that result in missorting and aberrant secretion of up to 95% of newly synthesized CPY. The CPY polypeptides synthesized by these mutants use the late secretory pathway to exit the cell, si...

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Bibliographic Details
Published inCell Vol. 48; no. 5; pp. 887 - 897
Main Authors Valls, Luis A., Hunter, Craig P., Rothman, Joel H., Stevens, Tom H.
Format Journal Article
LanguageEnglish
Published Cambridge, MA Elsevier Inc 13.03.1987
Cell Press
Subjects
Amino Acid Sequence
Base Sequence
Biological and medical sciences
Carboxypeptidases - genetics
Cathepsin A
DNA Restriction Enzymes
Enzyme Precursors - genetics
Fundamental and applied biological sciences. Psychology
Genes
Genes, Fungal
Growth, nutrition, metabolism, transports, enzymes. Molecular biology
Microbiology
Mutation
Mycology
Organoids - enzymology
Protein Processing, Post-Translational
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins
Vacuoles - enzymology
Intracellular transport
Property structure relationship
Yeast
Localization
Vacuole
Proteinase
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Summary:We have isolated cis-acting mutations in the gene encoding the yeast vacuolar protein carboxypeptidase Y (CPY) that result in missorting and aberrant secretion of up to 95% of newly synthesized CPY. The CPY polypeptides synthesized by these mutants use the late secretory pathway to exit the cell, since the late-acting sec1 mutation prevents their secretion. The mutant versions of CPY are secreted as the proCPY zymogen and are enzymatically activatable in vivo and in vitro. All the mutations, including small deletions and an amino acid substitution, map to the amino-terminal propeptide region and define a discrete yeast vacuolar localization domain whose integrity is required for efficient sorting of the CPY zymogen. Thus, the N-terminal propeptide of CPY carries out at least three functions: it mediates translocation across the endoplasmic reticulum, renders the enzyme inactive during transit, and targets the molecule to the vacuole.
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ISSN:0092-8674
1097-4172
DOI:10.1016/0092-8674(87)90085-7