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The regulation and function of mammalian AMPK‐related kinases
Author(s) -
Bright N. J.,
Thornton C.,
Carling D.
Publication year - 2009
Publication title -
acta physiologica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.591
H-Index - 116
eISSN - 1748-1716
pISSN - 1748-1708
DOI - 10.1111/j.1748-1716.2009.01971.x
Subject(s) - ampk , kinase , protein kinase a , amp activated protein kinase , regulator , phosphorylation , protein serine threonine kinases , microbiology and biotechnology , protein kinase domain , chemistry , biology , biochemistry , gene , mutant
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.