Cooperation of molecular chaperones with the ubiquitin/proteasome system.

Molecular chaperones and energy-dependent proteases have long been viewed as opposing forces that control protein biogenesis. Molecular chaperones are specialized in protein folding, whereas energy-dependent proteases such as the proteasome mediate efficient protein degradation. Recent data, however, suggest that molecular chaperones directly cooperate with the ubiquitin/proteasome system during protein quality control in eukaryotic cells. Modulating the intracellular balance of protein folding and protein degradation may open new strategies for the treatment of human diseases that involve chaperone pathways such as cancer and diverse amyloid diseases.

• Publication year

  2004

• Venue

  Biochimica et Biophysica Acta

• Publication date

  2004-11-29

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/J.BBAMCR.2004.09.020PMID 15571814
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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