Quality control: linking retrotranslocation and degradation.
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.
Stirling
Colin J
CJ
Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK.
Lord
J Michael
JM
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
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