The α1 and α2 isoforms of the AMP‐activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro

FEBS Letters

Hardie, D.Grahame²  Woods, Angela¹  Carling, David¹  Scott, James¹  Salt, Ian² 

[1] MRC Molecular Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, DuCane Road, London W12 0NN, UK;Department of Biochemistry, The University, Dundee, DD1 4HN, UK

关键词: AMP-activated protein kinase;    Subunit isoform;    Specificity determinant;    Consensus sequence;    AMPK;    AMP-activated protein kinase;    AMPKK;    AMP-activated protein kinase kinase;    SAMS;    synthetic peptide substrate HMRSAMSGLHLVKRR;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(96)01209-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The AMP-activated protein kinase (AMPK) is a heterotrimeric complex composed of a catalytic subunit (a) and two regulatory subunits (β and γ). Two isoforms of the catalytic subunit (αl and (α2) have been identified. We show here that the αl- and α2-containing complexes contribute approximately equally to total AMPK activity in rat liver. Furthermore, expression of al or a2 with β and Y in mammalian cells demonstrates that both complexes have equal specific activity measured with the SAMS peptide. Using variant peptides, however, we show that al and a2 exhibit slightly different substrate preferences, which suggest that the two isoforms could play different physiological roles within the cell.

【 授权许可】

Unknown