RRC ID 3523
Author Mouysset J, Kähler C, Hoppe T.
Title A conserved role of Caenorhabditis elegans CDC-48 in ER-associated protein degradation.
Journal J Struct Biol
Abstract Protein degradation mediated by the ubiquitin/proteasome system is essential for the elimination of misfolded proteins from the endoplasmic reticulum (ER) to adapt to ER stress. It has been reported that the AAA ATPase p97/VCP/CDC48 is required in this pathway for protein dislocation across the ER membrane and subsequent ubiquitin dependent degradation by the 26S proteasome in the cytosol. Throughout ER-associated protein degradation, p97 cooperates with a binary Ufd1/Npl4-complex. In Caenorhabditis elegans two homologs of p97, designated CDC-48.1 and CDC-48.2, exist. Our results indicate that both p97 homologs interact with UFD-1/NPL-4 in a similar CDC-48(UFD-1/NPL-4) complex. RNAi mediated depletion of the corresponding genes induces ER stress resulting in hypersensitivity to conditions which induce increased levels of unfolded proteins in the ER lumen. Together, these data suggest an evolutionarily conserved retro-translocation machinery at the endoplasmic reticulum.
Volume 156(1)
Pages 41-9
Published 2006-10-1
DOI 10.1016/j.jsb.2006.02.015
PII S1047-8477(06)00070-0
PMID 16647269
MeSH Adenosine Triphosphatases / genetics Adenosine Triphosphatases / metabolism* Animals Caenorhabditis elegans Proteins / genetics Caenorhabditis elegans Proteins / metabolism* Cytosol / metabolism Endoplasmic Reticulum / enzymology* Endoplasmic Reticulum / genetics Female Phylogeny Proteasome Endopeptidase Complex / metabolism* Protein Folding RNA Interference Two-Hybrid System Techniques Ubiquitin / genetics Ubiquitin / metabolism*
IF 3.071
Times Cited 27
WOS Category BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
Resource
C.elegans tm544 tm659