Pkc1p modifies CPY* degradation in the ERAD pathway

Biochem Biophys Res Commun. 2005 Jul 1;332(2):357-61. doi: 10.1016/j.bbrc.2005.04.136.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases
  • Biodegradation, Environmental
  • Cell Cycle Proteins / metabolism*
  • Endoplasmic Reticulum / metabolism*
  • Glycoproteins / metabolism*
  • 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

Substances

  • Cell Cycle Proteins
  • Glycoproteins
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • PKC1 protein, S cerevisiae
  • Protein Kinase C
  • Adenosine Triphosphatases
  • CDC48 protein, S cerevisiae
  • Valosin Containing Protein