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http://purl.uniprot.org/citations/23212600http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23212600http://www.w3.org/2000/01/rdf-schema#comment"The receptor for activated C-kinase 1 (RACK1) is a conserved structural protein of 40S ribosomes. Strikingly, deletion of RACK1 in yeast homolog Asc1 is not lethal. Mammalian RACK1 also interacts with many nonribosomal proteins, hinting at several extraribosomal functions. A knockout mouse for RACK1 has not previously been described. We produced the first RACK1 mutant mouse, in which both alleles of RACK1 gene are defective in RACK1 expression (ΔF/ΔF), in a pure C57 Black/6 background. In a sample of 287 pups, we observed no ΔF/ΔF mice (72 expected). Dissection and genotyping of embryos at various stages showed that lethality occurs at gastrulation. Heterozygotes (ΔF/+) have skin pigmentation defects with a white belly spot and hypopigmented tail and paws. ΔF/+ have a transient growth deficit (shown by measuring pup size at P11). The pigmentation deficit is partly reverted by p53 deletion, whereas the lethality is not. ΔF/+ livers have mild accumulation of inactive 80S ribosomal subunits by polysomal profile analysis. In ΔF/+ fibroblasts, protein synthesis response to extracellular and pharmacological stimuli is reduced. These results highlight the role of RACK1 as a ribosomal protein converging signaling to the translational apparatus."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.org/dc/terms/identifier"doi:10.1007/s00018-012-1215-y"xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/author"Beugnet A."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/author"Gallo S."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/author"Biffo S."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/author"Sanvito F."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/author"Brina D."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/author"Magri L."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/author"Volta V."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/author"Calamita P."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/author"Pesce E."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/name"Cell Mol Life Sci"xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/pages"1439-1450"xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/title"RACK1 depletion in a mouse model causes lethality, pigmentation deficits and reduction in protein synthesis efficiency."xsd:string
http://purl.uniprot.org/citations/23212600http://purl.uniprot.org/core/volume"70"xsd:string
http://purl.uniprot.org/citations/23212600http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23212600
http://purl.uniprot.org/citations/23212600http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23212600
http://purl.uniprot.org/uniprot/P68040#attribution-1F955F6F75484E2B81A1FE38B1DCD11Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/23212600
http://purl.uniprot.org/uniprot/#_P68040-mappedCitation-23212600http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23212600
http://purl.uniprot.org/uniprot/P68040http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23212600