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http://purl.uniprot.org/citations/28602583http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28602583http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28602583http://www.w3.org/2000/01/rdf-schema#comment"Recent findings suggest that components of the classical cell death machinery also have important non-cell-death (non-apoptotic) functions in flies, nematodes, and mammals. However, the mechanisms for non-canonical caspase substrate recognition and proteolysis, and the direct roles for caspases in gene expression regulation, remain largely unclear. Here we report that CED-3 caspase and the Arg/N-end rule pathway cooperate to inactivate the LIN-28 pluripotency factor in seam cells, a stem-like cell type in Caenorhabditis elegans, thereby ensuring proper temporal cell fate patterning. Importantly, the caspase and the E3 ligase execute this function in a non-additive manner. We show that CED-3 caspase and the E3 ubiquitin ligase UBR-1 form a complex that couples their in vivo activities, allowing for recognition and rapid degradation of LIN-28 and thus facilitating a switch in developmental programs. The interdependence of these proteolytic activities provides a paradigm for non-apoptotic caspase-mediated protein inactivation."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2017.05.013"xsd:string
http://purl.uniprot.org/citations/28602583http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2017.05.013"xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/author"Han M."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/author"Han M."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/author"Mitani S."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/author"Mitani S."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/author"Weaver B.P."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/author"Weaver B.P."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/author"Weaver Y.M."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/author"Weaver Y.M."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/pages"665-673"xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/pages"665-673"xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/title"Coupled Caspase and N-End Rule Ligase Activities Allow Recognition and Degradation of Pluripotency Factor LIN-28 during Non-Apoptotic Development."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/title"Coupled Caspase and N-End Rule Ligase Activities Allow Recognition and Degradation of Pluripotency Factor LIN-28 during Non-Apoptotic Development."xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/volume"41"xsd:string
http://purl.uniprot.org/citations/28602583http://purl.uniprot.org/core/volume"41"xsd:string
http://purl.uniprot.org/citations/28602583http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28602583
http://purl.uniprot.org/citations/28602583http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28602583