Conserved regulatory elements in AMPK

Lei Chen, Feng-Jiao Xin, Jue Wang, Jicheng Hu, Yuan-Yuan Zhang, Shuo Wan, Lu-Sha Cao, Chang Lu, Peng Li, S. Frank Yan, Dietbert Neumann, Uwe Schlattner, Bin Xia, Zhi-Xin Wang and Jia-Wei Wu ()
Additional contact information
Lei Chen: MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University
Feng-Jiao Xin: MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University
Jue Wang: MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University
Jicheng Hu: Beijing Nuclear Magnetic Resonance Center, College of Life Sciences, and College of Chemistry and Molecular Engineering, Peking University
Yuan-Yuan Zhang: MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University
Shuo Wan: Beijing Nuclear Magnetic Resonance Center, College of Life Sciences, and College of Chemistry and Molecular Engineering, Peking University
Lu-Sha Cao: MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University
Chang Lu: MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University
Peng Li: MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University
S. Frank Yan: Molecular Design and Biostructure, Roche Pharma Research and Early Development China
Dietbert Neumann: Cardiovascular Research Institute Maastricht, Maastricht University, 6200 MD Maastricht, The Netherlands
Uwe Schlattner: INSERM U1055, 38041 Grenoble Cedex 9, France
Bin Xia: Beijing Nuclear Magnetic Resonance Center, College of Life Sciences, and College of Chemistry and Molecular Engineering, Peking University
Zhi-Xin Wang: MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University
Jia-Wei Wu: MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University

Nature, 2013, vol. 498, issue 7453, E8-E10

Abstract: Abstract arising from B. Xiao et al. Nature 472, 230–233 (2011)10.1038/nature09932 The AMP-activated protein kinase (AMPK), an αβγ heterotrimeric enzyme, has a central role in regulating cellular metabolism and energy homeostasis1. The α-subunit of AMPK possesses the catalytic kinase domain, followed by a regulatory region comprising the autoinhibitory domain (AID) and α-linker2,3. Structural and biochemical studies suggested that AID is central to mammalian AMPK regulation4; however, this notion has been challenged recently by Xiao et al. on the basis of their active AMPK structure (Protein Data Bank accession 2Y94)5. On close inspection, however, we found that the α-subunit regulatory region was incorrectly built in their model, and our rebuilt model suggests a universal occurrence of the AID domain in AMPKs; we have also identified a novel regulatory motif that is essential for AMPK regulation.

Date: 2013
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature12189 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:498:y:2013:i:7453:d:10.1038_nature12189

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature12189

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().