| http://purl.uniprot.org/citations/11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11340163 | http://www.w3.org/2000/01/rdf-schema#comment | "Periodic activity of the anaphase-promoting complex (APC) ubiquitin ligase determines progression through multiple cell cycle transitions by targeting cell cycle regulators for destruction. At the G(1)/S transition, phosphorylation-dependent dissociation of the Cdh1-activating subunit inhibits the APC, allowing stabilization of proteins required for subsequent cell cycle progression. Cyclin-dependent kinases (CDKs) that initiate and maintain Cdh1 phosphorylation have been identified. However, the issue of which cyclin-CDK complexes are involved has been a matter of debate, and the mechanism of how cyclin-CDKs interact with APC subunits remains unresolved. Here we substantiate the evidence that mammalian cyclin A-Cdk2 prevents unscheduled APC reactivation during S phase by demonstrating its periodic interaction with Cdh1 at the level of endogenous proteins. Moreover, we identified a conserved cyclin-binding motif within the Cdh1 WD-40 domain and show that its disruption abolished the Cdh1-cyclin A-Cdk2 interaction, eliminated Cdh1-associated histone H1 kinase activity, and impaired Cdh1 phosphorylation by cyclin A-Cdk2 in vitro and in vivo. Overexpression of cyclin binding-deficient Cdh1 stabilized the APC-Cdh1 interaction and induced prolonged cell cycle arrest at the G(1)/S transition. Conversely, cyclin binding-deficient Cdh1 lost its capability to support APC-dependent proteolysis of cyclin A but not that of other APC substrates such as cyclin B and securin Pds1. Collectively, these data provide a mechanistic explanation for the mutual functional interplay between cyclin A-Cdk2 and APC-Cdh1 and the first evidence that Cdh1 may activate the APC by binding specific substrates."xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.21.11.3692-3703.2001"xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/author | "Peters J.M."xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/author | "Lukas C."xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/author | "Lukas J."xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/author | "Bartek J."xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/author | "Kramer E.R."xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/author | "Sorensen C.S."xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/name | "Mol Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/pages | "3692-3703"xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/title | "A conserved cyclin-binding domain determines functional interplay between anaphase-promoting complex-Cdh1 and cyclin A-Cdk2 during cell cycle progression."xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://purl.uniprot.org/core/volume | "21"xsd:string |
| http://purl.uniprot.org/citations/11340163 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11340163 |
| http://purl.uniprot.org/citations/11340163 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11340163 |
| http://purl.uniprot.org/uniprot/#_P51965-mappedCitation-11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11340163 |
| http://purl.uniprot.org/uniprot/#_Q13042-mappedCitation-11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11340163 |
| http://purl.uniprot.org/uniprot/#_P20248-mappedCitation-11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11340163 |
| http://purl.uniprot.org/uniprot/#_P51668-mappedCitation-11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11340163 |
| http://purl.uniprot.org/uniprot/#_O00762-mappedCitation-11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11340163 |
| http://purl.uniprot.org/uniprot/#_P46527-mappedCitation-11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11340163 |
| http://purl.uniprot.org/uniprot/#_P30260-mappedCitation-11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11340163 |
| http://purl.uniprot.org/uniprot/#_P24941-mappedCitation-11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11340163 |
| http://purl.uniprot.org/uniprot/#_P38936-mappedCitation-11340163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11340163 |