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dc.contributor.authorViana, Rosa-
dc.contributor.authorTowler, Mhairi-
dc.contributor.authorPan, David A.-
dc.contributor.authorCarling, David-
dc.contributor.authorViollet, Benoit-
dc.contributor.authorHardie, D. Grahame-
dc.contributor.authorSanz, Pascual-
dc.identifier.citationJ Biol Chem. 2007 June 1; 282(22): 16117–16125.en_US
dc.descriptionCopyright © by The American Society for Biochemistry and Molecular Biologyen_US
dc.description.abstractMammalian 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.en_US
dc.description.sponsorshipThis study was supported by the EXGENESIS Integrated Project (LSHM-CT-2004-005272) funded by the European Commission. Studies in the PS laboratory were also supported by the Spanish Ministry of Education and Science grant SAF2005-00852. Studies in the DGH laboratory were also supported by a Programme Grant from the Wellcome Trust.en_US
dc.format.extent1166196 bytes-
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen_US
dc.subjectAMP-activated protein kinaseen_US
dc.subjectGamma subunitsen_US
dc.subjectProtein-protein interactionen_US
dc.subjectTwo-hybrid analysisen_US
dc.subjectBateman domainen_US
dc.titleA conserved sequence immediatelly N-terminal to the bateman domains in AMP-activated protein kinase gamma subunits is required for the interaction with the beta subunitsen_US
dc.description.peerreviewedPeer revieweden_US
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