Structural basis of AMPK regulation by adenine nucleotides and glycogen
Abstract
AMP-activated protein kinase (AMPK) is a central cellular energy sensor and regulator of energy homeostasis, and a promising drug target for the treatment of diabetes, obesity, and cancer. Here we present low-resolution crystal structures of the human α1β2γ1 holo-AMPK complex bound to its allosteric modulators AMP and the glycogen-mimic cyclodextrin, both in the phosphorylated (4.05 Å) and non-phosphorylated (4.60 Å) state. In addition, we have solved a 2.95 Å structure of the human kinase domain (KD) bound to the adjacent autoinhibitory domain (AID) and have performed extensive biochemical and mutational studies. Altogether, these studies illustrate an underlying mechanism of allosteric AMPK modulation by AMP and glycogen, whose binding changes the equilibria between alternate AID (AMP) and carbohydrate-binding module (glycogen) interactions.
- Authors:
-
- Chinese Academy of Sciences, Guangdong (China); Univ. of Science and Technology of China, Anhui (China); Van Andel Research Institute, Grand Rapids, MI (United States)
- Van Andel Research Institute, Grand Rapids, MI (United States)
- Van Andel Research Institute, Grand Rapids, MI (United States); National Univ. of Singapore (Singapore)
- Chinese Academy of Sciences, Guangdong (China)
- Van Andel Research Institute, Grand Rapids, MI (United States); Chinese Academy of Sciences, Shanghai (China)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1169343
- Grant/Contract Number:
- AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Cell Research
- Additional Journal Information:
- Journal Volume: 25; Journal Issue: 1; Journal ID: ISSN 1001-0602
- Publisher:
- Shanghai Institutes for Biological Sciences
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; AMPK; adenine nucleotides; glycogen; diabetes
Citation Formats
Li, Xiaodan, Wang, Lili, Zhou, X. Edward, Ke, Jiyuan, de Waal, Parker W., Gu, Xin, Tan, M. H. Eileen, Wang, Dongye, Wu, Donghai, Xu, H. Eric, and Melcher, Karsten. Structural basis of AMPK regulation by adenine nucleotides and glycogen. United States: N. p., 2014.
Web. doi:10.1038/cr.2014.150.
Li, Xiaodan, Wang, Lili, Zhou, X. Edward, Ke, Jiyuan, de Waal, Parker W., Gu, Xin, Tan, M. H. Eileen, Wang, Dongye, Wu, Donghai, Xu, H. Eric, & Melcher, Karsten. Structural basis of AMPK regulation by adenine nucleotides and glycogen. United States. https://doi.org/10.1038/cr.2014.150
Li, Xiaodan, Wang, Lili, Zhou, X. Edward, Ke, Jiyuan, de Waal, Parker W., Gu, Xin, Tan, M. H. Eileen, Wang, Dongye, Wu, Donghai, Xu, H. Eric, and Melcher, Karsten. Fri .
"Structural basis of AMPK regulation by adenine nucleotides and glycogen". United States. https://doi.org/10.1038/cr.2014.150. https://www.osti.gov/servlets/purl/1169343.
@article{osti_1169343,
title = {Structural basis of AMPK regulation by adenine nucleotides and glycogen},
author = {Li, Xiaodan and Wang, Lili and Zhou, X. Edward and Ke, Jiyuan and de Waal, Parker W. and Gu, Xin and Tan, M. H. Eileen and Wang, Dongye and Wu, Donghai and Xu, H. Eric and Melcher, Karsten},
abstractNote = {AMP-activated protein kinase (AMPK) is a central cellular energy sensor and regulator of energy homeostasis, and a promising drug target for the treatment of diabetes, obesity, and cancer. Here we present low-resolution crystal structures of the human α1β2γ1 holo-AMPK complex bound to its allosteric modulators AMP and the glycogen-mimic cyclodextrin, both in the phosphorylated (4.05 Å) and non-phosphorylated (4.60 Å) state. In addition, we have solved a 2.95 Å structure of the human kinase domain (KD) bound to the adjacent autoinhibitory domain (AID) and have performed extensive biochemical and mutational studies. Altogether, these studies illustrate an underlying mechanism of allosteric AMPK modulation by AMP and glycogen, whose binding changes the equilibria between alternate AID (AMP) and carbohydrate-binding module (glycogen) interactions.},
doi = {10.1038/cr.2014.150},
journal = {Cell Research},
number = 1,
volume = 25,
place = {United States},
year = {Fri Nov 21 00:00:00 EST 2014},
month = {Fri Nov 21 00:00:00 EST 2014}
}
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Hierarchical activation of compartmentalized pools of AMPK depends on severity of nutrient or energy stress
journal, April 2019
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Methyl-β-cyclodextrin restores impaired autophagy flux in Niemann-Pick C1-deficient cells through activation of AMPK
text, January 2019
- Dai, Sheng; Dulcey, Andrés E.; Hu, Xin
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DNA-dependent protein kinase regulates lysosomal AMP-dependent protein kinase activation and autophagy
journal, January 2020
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The strange case of AMPK and cancer: Dr Jekyll or Mr Hyde?
journal, July 2019
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Reciprocal Association between the Apical Junctional Complex and AMPK: A Promising Therapeutic Target for Epithelial/Endothelial Barrier Function?
journal, November 2019
- Tsukita, Kazuto; Yano, Tomoki; Tamura, Atsushi
- International Journal of Molecular Sciences, Vol. 20, Issue 23
Conformational heterogeneity of the allosteric drug and metabolite (ADaM) site in AMP-activated protein kinase (AMPK)
journal, September 2018
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AMP-Activated Protein Kinase
journal, May 2017
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Fyn phosphorylates AMPK to inhibit AMPK activity and AMP-dependent activation of autophagy
journal, September 2016
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Deconvoluting AMP-activated protein kinase (AMPK) adenine nucleotide binding and sensing
journal, June 2017
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The strange case of AMPK and cancer: Dr Jekyll or Mr Hyde?
journal, July 2019
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Structure and Physiological Regulation of AMPK
journal, November 2018
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