Endocrine resistance and breast cancer plasticity are controlled by CoREST

Nat Struct Mol Biol. 2022 Nov;29(11):1122-1135. doi: 10.1038/s41594-022-00856-x. Epub 2022 Nov 7.

Abstract

Resistance to cancer treatment remains a major clinical hurdle. Here, we demonstrate that the CoREST complex is a key determinant of endocrine resistance and ER+ breast cancer plasticity. In endocrine-sensitive cells, CoREST is recruited to regulatory regions co-bound to ERα and FOXA1 to regulate the estrogen pathway. In contrast, during temporal reprogramming towards a resistant state, CoREST is recruited to AP-1 sites. In reprogrammed cells, CoREST favors chromatin opening, cJUN binding to chromatin, and gene activation by controlling SWI/SNF recruitment independently of the demethylase activity of the CoREST subunit LSD1. Genetic and pharmacological CoREST inhibition reduces tumorigenesis and metastasis of endocrine-sensitive and endocrine-resistant xenograft models. Consistently, CoREST controls a gene signature involved in invasiveness in clinical breast tumors resistant to endocrine therapies. Our studies reveal CoREST functions that are co-opted to drive cellular plasticity and resistance to endocrine therapies and tumorigenesis, thus establishing CoREST as a potential therapeutic target for the treatment of advanced breast cancer.

Publication types

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

MeSH terms

  • Breast Neoplasms* / drug therapy
  • Breast Neoplasms* / genetics
  • Breast Neoplasms* / pathology
  • Carcinogenesis
  • Chromatin
  • Co-Repressor Proteins / genetics
  • Co-Repressor Proteins / metabolism
  • Female
  • Histone Demethylases / genetics
  • Histone Demethylases / metabolism
  • Humans
  • Nerve Tissue Proteins / metabolism

Substances

  • Co-Repressor Proteins
  • Histone Demethylases
  • Nerve Tissue Proteins
  • Chromatin