Isolation of autophagocytosis mutants of Saccharomyces cerevisiae

  title={Isolation of autophagocytosis mutants of Saccharomyces cerevisiae},
  author={Michael Thumm and Ralf Egner and Bruce D. Koch and Martin Schlumpberger and Michael Straub and Marten Veenhuis and Dieter Heinrich Wolf},
  journal={FEBS Letters},
Autophagosome formation in mammalian cells.
Identification and characterization of the mammalian counterparts of the yeast autophagy proteins has facilitated understanding of mammalian autophapy, particularly of autophagosome formation, and these findings are now being applied to studies on the physiological roles of Autophagy in mammals.
Saccharomyces cerevisiae--a model organism for the studies on vacuolar transport.
An overview of the current knowledge of vesicle mediated vacuolar transport in the yeast Saccharomyces cerevisiae cells is provided.
From lysosome to proteasome: the power of yeast in the dissection of proteinase function in cellular regulation and waste disposal.
  • D. Wolf
  • Biology, Chemistry
    Cellular and molecular life sciences : CMLS
  • 2004
The function of vacuolar (lysosomal) proteolysis was elucidated and the in vivo role of ubiquitin and its relation to the proteasome was uncovered, providing surprising new insights in cellular control in health and disease.
Structure and function of the yeast vacuole and its role in autophagy
  • M. Thumm
  • Biology
    Microscopy research and technique
  • 2000
In this review, starvation‐induced autophagy and its relationship to the specific cytoplasm to vacuole targeting (cvt‐) pathway of proaminopeptidase I is discussed and the specific vacuolar uptake and degradation of peroxisomes in Pichia pastoris cells via micro‐ and macroautophagy is discussed.
Turnover of organelles by autophagy in yeast.
AUT 1 , a Gene Essential for Autophagocytosis in the Yeast Saccharomyces cerevisiae
Deletion of the AUT1 gene had no obvious influence on secretion, fluid phase endocytosis, or vacuolar protein sorting, which supports the idea of autophagocytotic as being a novel route transporting proteins from the cytoplasm to the vacuole.
The Core Molecular Machinery of Autophagosome Formation
This chapter summarizes knowledge about the roles and regulation of these core machinery components in autophagosome formation, in both yeast and mammalian systems.


Regulated import and degradation of a cytosolic protein in the yeast vacuole
The key regulatory enzyme in gluconeogenesis, fructose 1,6-bisphosphatase (FBPase) is subject to glucose-stimulated proteolytic degradation in Saccharomyces cerevisiae and may regulate the production of an FBPase receptor or import factor that is transported to the vacuole through the secretory pathway.
Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction
Accumulation of autophagic bodies in the vacuoles was induced not only by nitrogen starvation, but also by depletion of nutrients such as carbon and single amino acids that caused cessation of the cell cycle.
Biogenesis of the yeast vacuole (lysosome). Mutation in the active site of the vacuolar serine proteinase yscB abolishes proteolytic maturation of its 73-kDa precursor to the 41.5-kDa pro-enzyme and a newly detected 41-kDa peptide.
It is found that, in addition to pro-PrB, a distinct protein (superpeptide) with a mobility of about 41 kDa in SDS/PAGE is generated in the endoplasmic reticulum, and Pulse-chase experiments indicate rapid degradation of the 41-kDa superpeptides in wild-type cells.
Biogenesis of the yeast vacuole (lysosome). Proteinase yscB contributes molecularly and kinetically to vacuolar hydrolase-precursor maturation.
A molecular and kinetic participation of proteinase yscB in vacuolar hydrolase precursor maturation is indicated and is shown to trigger maturation of its 42-kDa pro-PrB precursor to mature PrB in the absence of PrA.
Three proteolytic systems in the yeast saccharomyces cerevisiae.
  • E. W. Jones
  • Biology, Chemistry
    The Journal of biological chemistry
  • 1991