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Oxygen Stress: A Regulator of Apoptosis in Yeast
TLDR
It is found that apoptosis can be induced in the yeast Saccharomyces cerevisiae by depletion of glutathione or by low external doses of H2O2, and oxygen radicals to accumulate in the cell, whereas radical depletion or hypoxia prevents apoptosis.
Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast.
TLDR
In DER1‐deleted cells, a substrate protein for ER degradation is retained in the ER by the same mechanism which also retains lumenal ER residents, which suggests that D ER1 acts in a process that directly removes protein from the folding environment of the ER.
Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
TLDR
Functional evidence from genetic studies is presented that Sec61p mediates retrograde transport of a mutated lumenal yeast carboxypeptidase ycsY (CPY*) in vivo and this work considers the export of endoplasmic reticulum-localized proteins to the cytosol by the translocon for proteasome degradation to be a general process in eukaryotic cell biology.
ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway
TLDR
The ER degradation system was studied with yeast mutants defective in the breakdown of a mutated soluble vacuolar protein, carboxypeptidase yscY (CPY*), where it is likely that CPY* entered the ER, was glycosylated, and was then transported out of the ER lumen to the cytoplasmic side of the organelle, where it was conjugated with ubiquitin and degraded.
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
TLDR
It is shown that short ubiquitin chains synthesized on proteolytic substrates are not sufficient to complete dislocation; the size of the chain seems to be a critical determinant.
The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca2+ and Mn2+ required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation.
TLDR
It is shown here that addition of Mn2+ greatly alleviates defects of pmr1 mutants in N-linked and O-linked protein glycosylation, and establishes a novel role of this secretory pathway pump in endoplasmic reticulum-associated processes.
Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation.
TLDR
The retro-translocon seems to be build up at least by the Sec61 pore, Der3p/Hrd1p and Hrd3p and mediates both retrograde transport and ubiquitination of substrates of the endoplasmic reticulum degradation machinery.
For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin–proteasome connection
TLDR
The endoplasmic reticulum (ER) is the organelle responsible for proper folding and delivery of proteins to the secretory pathway and contains a sophisticated protein proofreading and elimination mechanism.
Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins.
TLDR
Der3p might serve as a component programming the translocon for retrograde transport of ER proteins, or it might be involved in recognition through its lumenal RING-H2 motif of proteins of the ER that are destined for degradation.
Endoplasmic Reticulum Degradation of a Mutated ATP-binding Cassette Transporter Pdr5 Proceeds in a Concerted Action of Sec61 and the Proteasome*
TLDR
The data suggest that ER degradation is a mechanistically highly integrated process, requiring the combined operation of components of the degradation system acting at the lumenal face of the ER membrane, the Sec61 translocon, and the ubiquitin-proteasome system.
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