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

Mol Cell Biol. 1996 Jun;16(6):2700-7. doi: 10.1128/MCB.16.6.2700.

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

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alkaline Phosphatase / genetics
  • Alkaline Phosphatase / metabolism
  • Amino Acid Sequence
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Genes, Fungal*
  • Genetic Complementation Test
  • Golgi Apparatus / metabolism*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Mutation
  • Peptidyl-Dipeptidase A / genetics
  • Peptidyl-Dipeptidase A / metabolism
  • Phenotype
  • Protein Processing, Post-Translational
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism*
  • Vacuoles / metabolism

Substances

  • Fungal Proteins
  • Membrane Proteins
  • Recombinant Fusion Proteins
  • Alkaline Phosphatase
  • Peptidyl-Dipeptidase A