| http://purl.uniprot.org/citations/12172554 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12172554 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12172554 | http://www.w3.org/2000/01/rdf-schema#comment | "The direct mechanism by which the serine/threonine kinase Akt (also known as protein kinase B (PKB)) regulates cell growth is unknown. Here, we report that Drosophila melanogaster Akt/PKB stimulates growth by phosphorylating the tuberous sclerosis complex 2 (Tsc2) tumour suppressor and inhibiting formation of a Tsc1-Tsc2 complex. We show that Akt/PKB directly phosphorylates Drosophila Tsc2 in vitro at the conserved residues, Ser 924 and Thr 1518. Mutation of these sites renders Tsc2 insensitive to Akt/PKB signalling, increasing the stability of the Tsc1-Tsc2 complex within the cell. Stimulating Akt/PKB signalling in vivo markedly increases cell growth/size, disrupts the Tsc1-Tsc2 complex and disturbs the distinct subcellular localization of Tsc1 and Tsc2. Furthermore, all Akt/PKB growth signals are blocked by expression of a Tsc2 mutant lacking Akt phosphorylation sites. Thus, Tsc2 seems to be the critical target of Akt in mediating growth signals for the insulin signalling pathway."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb840"xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb840"xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/author | "Xu T."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/author | "Xu T."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/author | "Pedraza L.G."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/author | "Pedraza L.G."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/author | "Potter C.J."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/author | "Potter C.J."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/pages | "658-665"xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/pages | "658-665"xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/title | "Akt regulates growth by directly phosphorylating Tsc2."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/title | "Akt regulates growth by directly phosphorylating Tsc2."xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/volume | "4"xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://purl.uniprot.org/core/volume | "4"xsd:string |
| http://purl.uniprot.org/citations/12172554 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12172554 |
| http://purl.uniprot.org/citations/12172554 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12172554 |
| http://purl.uniprot.org/citations/12172554 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12172554 |
| http://purl.uniprot.org/citations/12172554 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12172554 |