1. DSpace at MEDIU
  2. Harvested articles مقالات مستوردة من مؤسسات وجامعات عالمية
  3. Digital Csic
Please use this identifier to cite or link to this item: http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3584
Full metadata record
DC FieldValueLanguage
dc.creatorViana, Rosa-
dc.creatorTowler, Mhairi-
dc.creatorPan, David A.-
dc.creatorCarling, David-
dc.creatorViollet, Benoit-
dc.creatorHardie, D. Grahame-
dc.creatorSanz, Pascual-
dc.date2008-04-15T10:27:53Z-
dc.date2008-04-15T10:27:53Z-
dc.date2007-04-02-
dc.date.accessioned2017-01-31T01:02:19Z-
dc.date.available2017-01-31T01:02:19Z-
dc.identifierJ Biol Chem. 2007 June 1; 282(22): 16117–16125.-
dc.identifier0021-9258-
dc.identifierhttp://hdl.handle.net/10261/3584-
dc.identifier10.1074/jbc.M611804200-
dc.identifier.urihttp://dspace.mediu.edu.my:8181/xmlui/handle/10261/3584-
dc.descriptionCopyright © by The American Society for Biochemistry and Molecular Biology-
dc.descriptionMammalian 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.-
dc.descriptionThis 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.-
dc.descriptionPeer reviewed-
dc.format1166196 bytes-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherAmerican Society for Biochemistry and Molecular Biology-
dc.rightsopenAccess-
dc.subjectAMP-activated protein kinase-
dc.subjectGamma subunits-
dc.subjectProtein-protein interaction-
dc.subjectTwo-hybrid analysis-
dc.subjectCo-immunoprecipitation-
dc.subjectBateman domain-
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 subunits-
dc.typeArtículo-
Appears in Collections:Digital Csic

Files in This Item:
There are no files associated with this item.
Show simple item record


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.