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A conserved sequence immediatelly N-terminal to the bateman domains in AMP-activated protein kinase gamma subunits is required for the interaction with the beta subunits

AutorViana, Rosa ; Towler, Mhairi; Pan, David A.; Carling, David; Viollet, Benoit; Hardie, D. Grahame; Sanz, Pascual
Palabras claveAMP-activated protein kinase
Gamma subunits
Protein-protein interaction
Two-hybrid analysis
Co-immunoprecipitation
Bateman domain
Fecha de publicación2-abr-2007
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJ Biol Chem. 2007 June 1; 282(22): 16117–16125.
ResumenMammalian AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that acts as a sensor of cellular energy status. AMPK is a heterotrimer of three different subunits, i.e. α, β and γ, with α being the catalytic subunit and β and γ having regulatory roles. Although several studies have defined different domains in α and β involved in the interaction with the other subunits of the complex, little is known about the regions of the γ subunits involved in these interactions. To study this, we have made sequential deletions from the N-termini of the γ subunit isoforms and studied the interactions with α and β subunits, both by two hybrid analysis and by co-immunoprecipitation. Our results suggest that a conserved region of 20-25 amino acids in γ1, γ2 and γ3, immediately N-terminal to the Bateman domains, is required for the formation of a functional, active αβγ complex. This region is required for the interaction with the β subunits. The interaction between the α and γ subunits does not require this region and occurs instead within the Bateman domains of the γ subunit, although the α-γ interaction does appear to stabilize the β-γ interaction. In addition, sequential deletions from the C-termini of the γ subunits indicate that deletion of any of the CBS motifs prevents the formation of a functional complex with the α and β subunits.
DescripciónCopyright © by The American Society for Biochemistry and Molecular Biology
URIhttp://hdl.handle.net/10261/3584
DOI10.1074/jbc.M611804200
ISSN0021-9258
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