title: Protein quality control: chaperones culling corrupt conformations.
abstract: Achieving the correct balance between folding and degradation of misfolded proteins is critical for cell viability. The importance of defining the mechanisms and factors that mediate cytoplasmic quality control is underscored by the growing list of diseases associated with protein misfolding and aggregation. Molecular chaperones assist protein folding and also facilitate degradation of misfolded polypeptides by the ubiquitin-proteasome system. Here we discuss emerging links between folding and degradation machineries and highlight challenges for future research.
authors.affiliation: Department of Biological Sciences and BioX Program, E200 Clark Center, Stanford University, Stanford, CA 94305, USA.
authors.forename: Amie J
authors.initials: AJ
authors.lastname: McClellan
authors.forename: Stephen
authors.initials: S
authors.lastname: Tam
authors.forename: Daniel
authors.initials: D
authors.lastname: Kaganovich
authors.forename: Judith
authors.initials: J
authors.lastname: Frydman
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000235:genetics; D006801:Humans; D008954:Models, Biological; D018832:Molecular Chaperones / Q000502:physiology*; D009154:Mutation / Q000235:genetics; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D043743:Ubiquitin-Protein Ligase Complexes / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism
chemical_list: D018832:Molecular Chaperones; D011506:Proteins; D043743:Ubiquitin-Protein Ligase Complexes; D044767:Ubiquitin-Protein Ligases; D046988:Proteasome Endopeptidase Complex