Pkc1p modifies CPY degradation in the ERAD pathway

The process of endoplasmic reticulum-associated degradation (ERAD) involved in the degradation of misfolded N-linked glycoproteins utilizes Cdc48p which extracts misfolded glycoproteins from the lumen to the cytosol to present them for deglycosylation and degradation. Pkc1p has been identified as a...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2005-07, Vol.332 (2), p.357-361
Main Authors: Nita-Lazar, Mihai, Lennarz, William J.
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases
Biodegradation, Environmental
Cdc48p
Cell Cycle Proteins - metabolism
Endoplasmic Reticulum - metabolism
Glycoprotein
Glycoproteins - metabolism
Misfolding
Protein Kinase C - metabolism
Protein Transport - physiology
Recombinant Proteins - metabolism
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Signal Transduction - physiology
Structure-Activity Relationship
Valosin Containing Protein
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Summary:The process of endoplasmic reticulum-associated degradation (ERAD) involved in the degradation of misfolded N-linked glycoproteins utilizes Cdc48p which extracts misfolded glycoproteins from the lumen to the cytosol to present them for deglycosylation and degradation. Pkc1p has been identified as a component of the ERAD pathway, because deletion of the pkc1 gene impairs ERAD and causes accumulation of CPY* in the lumen of the ER, most probably because of the mislocalization of Cdc48p. In addition, we show that Cdc48p interacts in the cytosol with the deglycosylation enzyme, PNGase, only when Cdc48p is associated with a misfolded glycoprotein.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2005.04.136