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PMID: 8649377 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The newly identified yeast GRD genes are required for retention of late-Golgi membrane proteins.

Molecular and cellular biology ·Vol. 16 ·No. 6 ·1996-06-00 ·Pages 2700-7

Nothwehr SF, Bryant NJ, Stevens TH

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

MeSH Terms
Alkaline Phosphatase/genetics,metabolism Amino Acid Sequence Fungal Proteins/genetics,metabolism Genes, Fungal Genetic Complementation Test Golgi Apparatus/metabolism Membrane Proteins/genetics,metabolism Molecular Sequence Data Mutation Peptidyl-Dipeptidase A/genetics,metabolism Phenotype Protein Processing, Post-Translational Recombinant Fusion Proteins/genetics,metabolism Saccharomyces cerevisiae/genetics,metabolism Vacuoles/metabolism
Chemicals
Fungal Proteins Membrane Proteins Recombinant Fusion Proteins Alkaline Phosphatase Peptidyl-Dipeptidase A
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Nothwehr S F
Division of Biological Sciences, University of Missouri, Columbia 65211, USA.
Bryant N J
Stevens T H
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1996-06-00
Pages
2700-7
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC231260
Subset
IM
Grants
NIGMS NIH HHS · GM 38006 · United States
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