The Regulation and Function of the NUAK Family
- X Sun, Department of Endocrinology, Provincial Hospital affiliated to Shandong University, Jinan, 250021, China
- L Gao, Central Laboratory, Provincial Hospital affiliated to Shandong University, Jinan, China
- H Chien, Department of Endocrinology & Metabolism, Taipei City Hospital, Taipei, Taiwan
- W Li, Department of Dentistry and Institute of Oral Biology, Taipei City Hospital, Taipei, Taiwan
- J Zhao, Department of Endocrinology, Provincial Hospital affiliated to Shandong University, Jinan, China
- Correspondence: Jiajun Zhao, Email: jjzhao{at}medmail.com
Abstract
AMP-activated protein kinase (AMPK) is a critical regulator of cellular and whole-body energy homeostasis. Twelve AMPK-related kinases (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 (UBA) domain and a C-terminal spacer sequence which in some cases also contains a kinase associated domain 1 (KA1). Eleven of the AMPK-related kinases are phosphorylated and activated by the master upstream kinase LKB1. However, most of these AMPK-related kinases 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.
- Received 22 October 2012
- Revision received 9 May 2013
- Accepted 14 May 2013
- Accepted Preprint first posted online on 19 July 2013
