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Conserved regulatory elements in AMPK

Author

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  • Lei Chen

    (MOE Key Laboratory of Protein Sciences and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University
    Present address: Vollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA)

  • 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
    Laboratory of Fundamental and Applied Bioenergetics, University Joseph Fourier, BP 53, 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)

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.

Suggested Citation

  • 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 & Jia-Wei Wu, 2013. "Conserved regulatory elements in AMPK," Nature, Nature, vol. 498(7453), pages 8-10, June.
    • Handle: RePEc:nat:nature:v:498:y:2013:i:7453:d:10.1038_nature12189
    DOI: 10.1038/nature12189
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    Cited by:

    1. Kamaran M. K. Mondal, 2015. "Canada’s Growing Interest in the Far Away West Asia," International Studies, , vol. 52(1-4), pages 27-37, January.

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