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Protein quality control: chaperones culling corrupt conformations

Nature Cell Biology volume 7, pages 736–741 (2005)Cite this article

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.

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Figure 1: Role of molecular chaperones in the balance of folding, degradation and aggregation.
Figure 2: Domain organization of selected proteins linking chaperones and the UPS.

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Acknowledgements

The authors thank J. Christianson, V. Albanese and R. Geller for their helpful comments and suggestions. We apologize to authors whose primary references we were unable to cite due to space limitations.

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Authors and Affiliations

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

    Amie J. McClellan, Stephen Tam, Daniel Kaganovich & Judith Frydman

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McClellan, A., Tam, S., Kaganovich, D. et al. Protein quality control: chaperones culling corrupt conformations. Nat Cell Biol 7, 736–741 (2005). https://doi.org/10.1038/ncb0805-736

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