Oestrogen receptors interact with the α-catalytic subunit of AMP-activated protein kinase

Yulia Lipovka, Hao Chen, Josef Vagner, Theodore J. Price, Tsu Shuen Tsao, John P. Konhilas

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


Normal and pathological stressors engage the AMP-activated protein kinase (AMPK) signalling axis to protect the cell from energetic pressures. Sex steroid hormones also play a critical role in energy metabolism and significantly modify pathological progression of cardiac disease, diabetes/obesity and cancer. AMPK is targeted by 17β-oestradiol (E2), the main circulating oestrogen, but the mechanism by which E2 activates AMPK is currently unknown. Using an oestrogen receptor α/β (ERα/β) positive (T47D) breast cancer cell line, we validated E2-dependent activation of AMPK that was mediated through ERα (not ERβ) by using three experimental strategies. A series of co-immunoprecipitation experiments showed that both ERs associated with AMPK in cancer and striated (skeletal and cardiac) muscle cells. We further demonstrated direct binding of ERs to the α-catalytic subunit of AMPK within the βγ-subunit-binding domain. Finally, both ERs interacted with the upstream liver kinase B 1 (LKB1) kinase complex, which is required for E2-dependent activation of AMPK. We conclude that E2 activates AMPK through ERα by direct interaction with the βγ-binding domain of AMPKα.

Original languageEnglish (US)
JournalBioscience reports
Issue number5
StatePublished - Sep 15 2015
Externally publishedYes


  • AMP-activated protein kinase (AMPK)
  • breast cancer
  • oestradiol
  • oestrogen receptors

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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