title: Quality control: linking retrotranslocation and degradation.
abstract: Misfolded proteins in the ER require the p97 AAA ATPase for dislocation across the membrane prior to degradation by the cytosolic proteasome. The mechanism by which dislocated proteins are delivered to the proteasome from p97 is unclear, but recent studies suggest an important regulatory role for the protein ataxin-3.
authors.affiliation: Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK.
authors.forename: Colin J
authors.initials: CJ
authors.lastname: Stirling
authors.forename: J Michael
authors.initials: JM
authors.lastname: Lord
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D000067699:Ataxin-3; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D017510:Protein Folding; D021381:Protein Transport; D011506:Proteins / Q000378:metabolism*; D012097:Repressor Proteins / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism
chemical_list: D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D011506:Proteins; D012097:Repressor Proteins; D025801:Ubiquitin; C092341:ATXN3 protein, human; D000067699:Ataxin-3; D046988:Proteasome Endopeptidase Complex; D000251:Adenosine Triphosphatases; C404942:p97 ATPase