Oestrogen Receptors Interact with the α-Catalytic Subunit of AMP-Activated Protein Kinase

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Oestrogen Receptors Interact with the α-Catalytic Subunit of AMP-Activated Protein Kinase

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Title: Oestrogen Receptors Interact with the α-Catalytic Subunit of AMP-Activated Protein Kinase
Author(s):
Lipovka, Yulia;
Chen, Hao;
Vagner, Josef;
Price, Theodore J. (UT Dallas);
Tsao, Tsu-Shuen;
Konhilas, John P.
Item Type: article
Keywords: Show Keywords
Description: Includes supplementary material
Abstract: Normal and pathological stressors engage the AMP-activated protein kinase (AMPK) signaling 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 by17β-estradiol (E2), the main circulating estrogen, but the mechanism by which E2 activates AMPK is currently unknown. Using an estrogen 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 LKB1 kinase complex, which is required for E2-dependent activation of AMPK. We conclude that estradiol activates AMPK through ERα by direct interaction with the βγ-binding domain of AMPKα.; Copyright 2015 The Author(s).
Publisher: Portland Press on behalf of the Biochemical Society
ISSN: 1573-4935
Persistent Link: http://hdl.handle.net/10735.1/5316
Bibliographic Citation: Lipovka, Yulia, Hao Chen, Josef Vagner, Theodore J. Price, et al. 2015. "Oestrogen receptors interact with the α-catalytic subunit of AMP-activated protein kinase." Bioscience Reports (2015), doi:10.1042/BSR20150074
Terms of Use: CC BY 3.0 (Attribution) License
©2015 The Authors
Sponsors: NIH grant [no. HL098256]; National Mentored Research Science Development Award [K01 AR052840] and Independent Scientist Award [no. K02 HL105799]; NIH/NCRR grant [no. 1S10 RR028868-01].

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