Surviving protein quality control catastrophes--from cells to organisms

Kim Schneider1, Anne Bertolotti2

  • 1MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.

Journal of Cell Science
|October 21, 2015
PubMed

Insights

Cells possess resilience to misfolded proteins, a key factor in neurodegenerative diseases. Understanding the limits of this cellular resilience may offer new strategies against age-related protein misfolding diseases.

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Neuroscience

Background:

  • Misfolded proteins pose a significant threat to cellular and organismal health.
  • Protein misfolding and aggregation are hallmarks of age-related neurodegenerative diseases.
  • Despite lifelong expression of aggregation-prone proteins, diseases manifest late, indicating inherent cellular resilience.

Purpose of the Study:

  • To outline the boundaries of cellular resilience against protein misfolding.
  • To explore methods for enhancing cellular resilience to protein misfolding.
  • To prevent protein quality control failures and associated diseases.

Main Methods:

  • This commentary reviews existing literature on cellular protein quality control mechanisms.
  • It analyzes the factors contributing to the failure of these mechanisms over time.
  • It discusses potential therapeutic strategies targeting cellular resilience.

Main Results:

  • Cells exhibit a finite capacity to manage misfolded proteins.
  • Aging and other factors can compromise cellular resilience.
  • Exceeding these limits can lead to protein quality control catastrophes and disease.

Conclusions:

  • Cellular resilience to protein misfolding is crucial for preventing neurodegenerative diseases.
  • Pushing the limits of cellular resilience could offer therapeutic benefits.
  • Further research into enhancing protein quality control is warranted to combat age-related diseases.

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