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Protein degradation and protection against misfolded or damaged proteins

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  • Alfred L. Goldberg

    (Harvard Medical School)

Abstract

The ultimate mechanism that cells use to ensure the quality of intracellular proteins is the selective destruction of misfolded or damaged polypeptides. In eukaryotic cells, the large ATP-dependent proteolytic machine, the 26S proteasome, prevents the accumulation of non-functional, potentially toxic proteins. This process is of particular importance in protecting cells against harsh conditions (for example, heat shock or oxidative stress) and in a variety of diseases (for example, cystic fibrosis and the major neurodegenerative diseases). A full understanding of the pathogenesis of the protein-folding diseases will require greater knowledge of how misfolded proteins are recognized and selectively degraded.

Suggested Citation

  • Alfred L. Goldberg, 2003. "Protein degradation and protection against misfolded or damaged proteins," Nature, Nature, vol. 426(6968), pages 895-899, December.
    • Handle: RePEc:nat:nature:v:426:y:2003:i:6968:d:10.1038_nature02263
    DOI: 10.1038/nature02263
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    Cited by:

    1. Jiangan Xie & Zhiling Xu & Shangbo Zhou & Xianchao Pan & Shaoxi Cai & Li Yang & Hu Mei, 2013. "The VHSE-Based Prediction of Proteasomal Cleavage Sites," PLOS ONE, Public Library of Science, vol. 8(9), pages 1-8, September.
    2. Naghshbandi, Mohammad Pooya & Tabatabaei, Meisam & Aghbashlo, Mortaza & Gupta, Vijai Kumar & Sulaiman, Alawi & Karimi, Keikhosro & Moghimi, Hamid & Maleki, Mina, 2019. "Progress toward improving ethanol production through decreased glycerol generation in Saccharomyces cerevisiae by metabolic and genetic engineering approaches," Renewable and Sustainable Energy Reviews, Elsevier, vol. 115(C).

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