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Nat Cell Biol. 2005 Aug;7(8):736-41.

Protein quality control: chaperones culling corrupt conformations.

Author information

1
Department of Biological Sciences and BioX Program, E200 Clark Center, Stanford University, Stanford, CA 94305, USA.

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.

PMID:
16056264
DOI:
10.1038/ncb0805-736
[Indexed for MEDLINE]

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