The regulation and function of the NUAK family

    1. Jiajun Zhao1
    1. 1Department of Endocrinology
      2Central Laboratory, Provincial Hospital affiliated to Shandong University, Jinan, China
      3Department of Endocrinology and Metabolism, Taipei City Hospital, Ren-Ai Branch, Taipei, Taiwan
      4Department of Dentistry, School of Dentistry, Institute of Oral Biology, National Yang-Ming University, Taipei, Taiwan
      5Department of Education and Research, Taipei City Hospital, Taipei, Taiwan
    1. Correspondence should be addressed to W-C Li or J Zhao; Email: wcli{at} or jjzhao{at}


    AMP-activated protein kinase (AMPK) is a critical regulator of cellular and whole-body energy homeostasis. Twelve AMPK-related kinases (ARKs; BRSK1, BRSK2, NUAK1, NUAK2, QIK, QSK, SIK, MARK1, MARK2, MARK3, MARK4, and MELK) have been identified recently. These kinases show a similar structural organization, including an N-terminal catalytic domain, followed by a ubiquitin-associated domain and a C-terminal spacer sequence, which in some cases also contains a kinase-associated domain 1. Eleven of the ARKs are phosphorylated and activated by the master upstream kinase liver kinase B1. However, most of these ARKs are largely unknown, and the NUAK family seems to have different regulations and functions. This review contains a brief discussion of the NUAK family including the specific characteristics of NUAK1 and NUAK2.

    • Revision received 9 May 2013
    • Accepted 19 July 2013
    • Made available online as an Accepted Preprint 19 July 2013
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