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http://purl.uniprot.org/citations/35929733http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35929733http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35929733http://www.w3.org/2000/01/rdf-schema#comment"The phagocytic receptor CED-1 mediates apoptotic cell recognition by phagocytic cells, enabling cell corpse clearance in Caenorhabditis elegans. Whether appropriate levels of CED-1 are maintained for executing the engulfment function remains unknown. Here, we identified the C. elegans E3 ubiquitin ligase tripartite motif containing-21 (TRIM-21) as a component of the CED-1 pathway for apoptotic cell clearance. When the NPXY motif of CED-1 was bound to the adaptor protein CED-6 or the YXXL motif of CED-1 was phosphorylated by tyrosine kinase SRC-1 and subsequently bound to the adaptor protein NCK-1 containing the SH2 domain, TRIM-21 functioned in conjunction with UBC-21 to catalyze K48-linked poly-ubiquitination on CED-1, targeting it for proteasomal degradation. In the absence of TRIM-21, CED-1 accumulated post-translationally and drove cell corpse degradation defects, as evidenced by direct binding to VHA-10. These findings reveal a unique mechanism for the maintenance of appropriate levels of CED-1 to regulate apoptotic cell clearance."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.org/dc/terms/identifier"doi:10.7554/elife.76436"xsd:string
http://purl.uniprot.org/citations/35929733http://purl.org/dc/terms/identifier"doi:10.7554/elife.76436"xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Jing H."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Jing H."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Yuan L."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Yuan L."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Zheng Q."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Zheng Q."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Xiao H."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/author"Xiao H."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/title"trim-21 promotes proteasomal degradation of CED-1 for apoptotic cell clearance in C. elegans."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/title"trim-21 promotes proteasomal degradation of CED-1 for apoptotic cell clearance in C. elegans."xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/35929733http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/35929733http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/35929733
http://purl.uniprot.org/citations/35929733http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/35929733