Abstract
Processing of A-ALP, a late-Golgi membrane protein constructed by fusing the cytosolic domain of dipeptidyl aminopeptidase A to the transmembrane and lumenal domains of alkaline phosphatase (ALP), serves as a convenient assay for loss of retention of late-Golgi membrane proteins in Saccharomyces cerevisiae. In this study, a large group of novel grd (for Golgi retention defective) yeast mutants, representing 18 complementation groups, were identified on the basis of their mislocalization of A-ALP to the vacuole, where it was proteolytically processed and thus became enzymatically activated. All of the grd mutants exhibited significant mislocalization of A-ALP, as measured by determining the kinetics of A-ALP processing and by analyzing its
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alkaline Phosphatase / genetics
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Alkaline Phosphatase / metabolism
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Amino Acid Sequence
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Genes, Fungal*
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Genetic Complementation Test
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Golgi Apparatus / metabolism*
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Mutation
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Peptidyl-Dipeptidase A / genetics
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Peptidyl-Dipeptidase A / metabolism
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Phenotype
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Protein Processing, Post-Translational
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / metabolism*
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Vacuoles / metabolism
Substances
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Fungal Proteins
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Membrane Proteins
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Recombinant Fusion Proteins
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Alkaline Phosphatase
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Peptidyl-Dipeptidase A