Protein quality control: chaperones culling corrupt conformations.
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.
McClellan
Amie J
AJ
Department of Biological Sciences and BioX Program, E200 Clark Center, Stanford University, Stanford, CA 94305, USA.
Tam
Stephen
S
Kaganovich
Daniel
D
Frydman
Judith
J
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
D018832:Molecular Chaperones; D011506:Proteins; D043743:Ubiquitin-Protein Ligase Complexes; D044767:Ubiquitin-Protein Ligases; D046988:Proteasome Endopeptidase Complex