| http://purl.uniprot.org/citations/23297348 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23297348 | http://www.w3.org/2000/01/rdf-schema#comment | "The conserved family of Cdc14 phosphatases targets cyclin-dependent kinase substrates in yeast, mediating late mitotic signaling events. To discover substrates and regulators of the Schizosaccharomyces pombe Cdc14 phosphatase Clp1, TAP-tagged Clp1, and a substrate trapping mutant (Clp1-C286S) were purified from asynchronous and mitotic (prometaphase and anaphase) cells and binding partners were identified by 2D-LC-MS/MS. Over 100 Clp1-interacting proteins were consistently identified, over 70 of these were enriched in Clp1-C286S-TAP (potential substrates) and we and others detected Cdk1 phosphorylation sites in over half (44/73) of these potential substrates. According to GO annotations, Clp1-interacting proteins are involved in many essential cellular processes including mitosis, cytokinesis, ribosome biogenesis, transcription, and trafficking among others. We confirmed association and dephosphorylation of multiple candidate substrates, including a key scaffolding component of the septation initiation network called Cdc11, an essential kinase of the conserved morphogenesis-related NDR kinase network named Shk1, and multiple Mlu1-binding factor transcriptional regulators. In addition, we identified Sal3, a nuclear β-importin, as the sole karyopherin required for Clp1 nucleoplasmic shuttling, a key mode of Cdc14 phosphatase regulation. Finally, a handful of proteins were more abundant in wild type Clp1-TAP versus Clp1-C286S-TAP, suggesting that they may directly regulate Clp1 signaling or serve as scaffolding platforms to localize Clp1 activity."xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.org/dc/terms/identifier | "doi:10.1074/mcp.m112.025924"xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/author | "Chen J.S."xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/author | "Ren L."xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/author | "Feoktistova A."xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/author | "Gould K.L."xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/author | "McLean J.R."xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/author | "Broadus M.R."xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/name | "Mol Cell Proteomics"xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/pages | "1074-1086"xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/title | "Comprehensive proteomics analysis reveals new substrates and regulators of the fission yeast clp1/cdc14 phosphatase."xsd:string |
| http://purl.uniprot.org/citations/23297348 | http://purl.uniprot.org/core/volume | "12"xsd:string |
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