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http://purl.uniprot.org/citations/25858807http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25858807http://www.w3.org/2000/01/rdf-schema#comment"Stresses like low nutrients, systemic inflammation, cancer or infections provoke a catabolic state characterized by enhanced muscle proteolysis and amino acid release to sustain liver gluconeogenesis and tissue protein synthesis. These conditions activate the family of Forkhead Box (Fox) O transcription factors. Here we report that muscle-specific deletion of FoxO members protects from muscle loss as a result of the role of FoxOs in the induction of autophagy-lysosome and ubiquitin-proteasome systems. Notably, in the setting of low nutrient signalling, we demonstrate that FoxOs are required for Akt activity but not for mTOR signalling. FoxOs control several stress-response pathways such as the unfolded protein response, ROS detoxification, DNA repair and translation. Finally, we identify FoxO-dependent ubiquitin ligases including MUSA1 and a previously uncharacterised ligase termed SMART (Specific of Muscle Atrophy and Regulated by Transcription). Our findings underscore the central function of FoxOs in coordinating a variety of stress-response genes during catabolic conditions."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.org/dc/terms/identifier"doi:10.1038/ncomms7670"xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Goldberg A.L."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Zhao J."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"DePinho R.A."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Sandri M."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Abraham R."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Blaauw B."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Romanello V."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Seydel A."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Milan G."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Armani A."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Paik J.H."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Frasson L."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/author"Pescatore F."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/pages"6670"xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/title"Regulation of autophagy and the ubiquitin-proteasome system by the FoxO transcriptional network during muscle atrophy."xsd:string
http://purl.uniprot.org/citations/25858807http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/25858807http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25858807
http://purl.uniprot.org/citations/25858807http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25858807
http://purl.uniprot.org/uniprot/#_A0A087WRZ7-mappedCitation-25858807http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25858807
http://purl.uniprot.org/uniprot/#_E0CZ30-mappedCitation-25858807http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25858807