Targeting protein quality control pathways in breast cancer

BMC Biol. 2017 Nov 16;15(1):109. doi: 10.1186/s12915-017-0449-4.

Abstract

The efficient production, folding, and secretion of proteins is critical for cancer cell survival. However, cancer cells thrive under stress conditions that damage proteins, so many cancer cells overexpress molecular chaperones that facilitate protein folding and target misfolded proteins for degradation via the ubiquitin-proteasome or autophagy pathway. Stress response pathway induction is also important for cancer cell survival. Indeed, validated targets for anti-cancer treatments include molecular chaperones, components of the unfolded protein response, the ubiquitin-proteasome system, and autophagy. We will focus on links between breast cancer and these processes, as well as the development of drug resistance, relapse, and treatment.

Publication types

  • Review
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autophagy*
  • Breast Neoplasms / genetics*
  • Female
  • Humans
  • Molecular Chaperones / metabolism*
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Folding
  • Protein Processing, Post-Translational*
  • Ubiquitin / metabolism*
  • Unfolded Protein Response

Substances

  • Molecular Chaperones
  • Ubiquitin
  • Proteasome Endopeptidase Complex