| http://purl.uniprot.org/citations/16847059 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16847059 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16847059 | http://www.w3.org/2000/01/rdf-schema#comment | "The Snf1 kinase and its mammalian orthologue, the AMP-activated protein kinase (AMPK), function as heterotrimers composed of a catalytic alpha-subunit and two non-catalytic subunits, beta and gamma. The beta-subunit is thought to hold the complex together and control subcellular localization whereas the gamma-subunit plays a regulatory role by binding to and blocking the function of an auto-inhibitory domain (AID) present in the alpha-subunit. In addition, catalytic activity requires phosphorylation by a distinct upstream kinase. In yeast, any one of three Snf1-activating kinases, Sak1, Tos3, or Elm1, can fulfill this role. We have previously shown that Sak1 is the only Snf1-activating kinase that forms a stable complex with Snf1. Here we show that the formation of the Sak1.Snf1 complex requires the beta- and gamma-subunits in vivo. However, formation of the Sak1.Snf1 complex is not necessary for glucose-regulated phosphorylation of the Snf1 activation loop. Snf1 kinase purified from cells lacking the beta-subunits do not contain any gamma-subunit, indicating that the Snf1 kinase does not form a stable alphagamma dimer in vivo. In vitro kinase assays using purified full-length and truncated Snf1 proteins demonstrate that the kinase domain, which lacks the AID, is significantly more active than the full-length Snf1 protein. Addition of purified beta- and gamma-subunits could stimulate the kinase activity of the full-length alpha-subunit but only when all three subunits were present, suggesting an interdependence of all three subunits for assembly of a functional complex."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m603811200"xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m603811200"xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/author | "Elbing K."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/author | "Elbing K."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/author | "McCartney R.R."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/author | "McCartney R.R."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/author | "Rubenstein E.M."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/author | "Rubenstein E.M."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/author | "Schmidt M.C."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/author | "Schmidt M.C."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/pages | "26170-26180"xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/pages | "26170-26180"xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/title | "Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/title | "Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity."xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/volume | "281"xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://purl.uniprot.org/core/volume | "281"xsd:string |
| http://purl.uniprot.org/citations/16847059 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16847059 |
| http://purl.uniprot.org/citations/16847059 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16847059 |