The regulation and function of mammalian AMPK-related kinases
Article first published online: 19 FEB 2009
© 2009 The Authors. Journal compilation © 2009 Scandinavian Physiological Society
Special Issue: THE 5TH INTERNATIONAL SYMPOSIUM ON AMPK 'AMPK IN SICKNESS AND HEALTH - FROM MOLECULE TO MAN'
Volume 196, Issue 1, pages 15–26, May 2009
How to Cite
Bright, N. J., Thornton, C. and Carling, D. (2009), The regulation and function of mammalian AMPK-related kinases. Acta Physiologica, 196: 15–26. doi: 10.1111/j.1748-1716.2009.01971.x
- Issue published online: 1 APR 2009
- Article first published online: 19 FEB 2009
- Received 1 September 2008, accepted 20 November 2008
- AMP-activated protein kinase;
- cell polarity;
AMP-activated protein kinase (AMPK) is a key regulator of cellular and whole-body energy homeostasis. Recently, 12 AMPK-related kinases (BRSK1, BRSK2, NUAK1, NUAK2, QIK, QSK, SIK, MARK1, MARK2, MARK3, MARK4 and MELK) were identified that are closely related by sequence homology to the catalytic domain of AMPK. The protein kinase LKB1 acts as a master upstream kinase activating AMPK and 11 of the AMPK-related kinases by phosphorylation of a conserved threonine residue in their T-loop region. Further sequence analyses have identified the eight-member SNRK kinase family as distant relatives of AMPK. However, only one of these is phosphorylated and activated by LKB1. Although much is known about AMPK, many of the AMPK-related kinases remain largely uncharacterized. This review outlines the general similarities in structure and function of the AMPK-related kinases before examining the specific characteristics of each, including a brief discussion of the SNRK family.