Protein rescue from aggregates by powerful molecular chaperone machines.
Protein quality control within the cell requires the interplay of many molecular chaperones and proteases. When this quality control system is disrupted, polypeptides follow pathways leading to misfolding, inactivity and aggregation. Among the repertoire of molecular chaperones are remarkable proteins that forcibly untangle protein aggregates, called disaggregases. Structural and biochemical studies have led to new insights into how these proteins collaborate with co-chaperones and utilize ATP to power protein disaggregation. Understanding how energy-dependent protein disaggregating machines function is universally important and clinically relevant, as protein aggregation is linked to medical conditions such as Alzheimer's disease, Parkinson's disease, amyloidosis and prion diseases.
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, 37 Convent Drive, Bldg. 37, Room 5144, Bethesda, Maryland 20892, USA.
Shannon M
SM
Doyle
Olivier
O
Genest
Sue
S
Wickner
D000544:Alzheimer Disease / Q000235:genetics / Q000473:pathology; D000686:Amyloidosis / Q000235:genetics / Q000473:pathology; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D010300:Parkinson Disease / Q000235:genetics / Q000473:pathology; D010447:Peptide Hydrolases / Q000378:metabolism*; D017096:Prion Diseases / Q000235:genetics* / Q000473:pathology; D011487:Protein Conformation; D017510:Protein Folding; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011786:Quality Control
D018832:Molecular Chaperones; D011506:Proteins; D010447:Peptide Hydrolases