| http://purl.uniprot.org/citations/16543145 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16543145 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16543145 | http://www.w3.org/2000/01/rdf-schema#comment | "We investigated the role of glycogen synthase kinase-3 (GSK-3), which is inactivated by AKT, for its role in the regulation of apoptosis. Upon IL-3 withdrawal, protein levels of MCL-1 decreased but were sustained by pharmacological inhibition of GSK-3, which prevented cytochrome c release and apoptosis. MCL-1 was phosphorylated by GSK-3 at a conserved GSK-3 phosphorylation site (S159). S159 phosphorylation of MCL-1 was induced by IL-3 withdrawal or PI3K inhibition and prevented by AKT or inhibition of GSK-3, and it led to increased ubiquitinylation and degradation of MCL-1. A phosphorylation-site mutant (MCL-1(S159A)), expressed in IL-3-dependent cells, showed enhanced stability upon IL-3 withdrawal and conferred increased protection from apoptosis compared to wild-type MCL-1. The results demonstrate that the control of MCL-1 stability by GSK-3 is an important mechanism for the regulation of apoptosis by growth factors, PI3K, and AKT."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2006.02.009"xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2006.02.009"xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Green D.R."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Green D.R."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Charvet C."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Charvet C."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Dejardin E."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Dejardin E."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Maurer U."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Maurer U."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Wagman A.S."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/author | "Wagman A.S."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/pages | "749-760"xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/pages | "749-760"xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/title | "Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/title | "Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1."xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/volume | "21"xsd:string |
| http://purl.uniprot.org/citations/16543145 | http://purl.uniprot.org/core/volume | "21"xsd:string |