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http://purl.uniprot.org/citations/30718913http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30718913http://www.w3.org/2000/01/rdf-schema#comment"N-myristoyltransferase (NMT) attaches the fatty acid myristate to the N-terminal glycine of proteins to sort them into soluble and membrane-bound fractions. Function of the energy-sensing AMP-activated protein kinase, AMPK, is myristoylation dependent. In rheumatoid arthritis (RA), pathogenic T cells shift glucose away from adenosine tri-phosphate production toward synthetic and proliferative programs, promoting proliferation, cytokine production, and tissue invasion. We found that RA T cells had a defect in NMT1 function, which prevented AMPK activation and enabled unopposed mTORC1 signaling. Lack of the myristate lipid tail disrupted the lysosomal translocation and activation of AMPK. Instead, myristoylation-incompetent RA T cells hyperactivated the mTORC1 pathway and differentiated into pro-inflammatory TH1 and TH17 helper T cells. In vivo, NMT1 loss caused robust synovial tissue inflammation, whereas forced NMT1 overexpression rescued AMPK activation and suppressed synovitis. Thus, NMT1 has tissue-protective functions by facilitating lysosomal recruitment of AMPK and dampening mTORC1 signaling."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.org/dc/terms/identifier"doi:10.1038/s41590-018-0296-7"xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Shen Y."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Yang Z."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Wu B."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Wen Z."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Tian L."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Jin K."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Goronzy J.J."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Weyand C.M."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Roche N.E."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/author"Shoor S."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/name"Nat Immunol"xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/pages"313-325"xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/title"N-myristoyltransferase deficiency impairs activation of kinase AMPK and promotes synovial tissue inflammation."xsd:string
http://purl.uniprot.org/citations/30718913http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/30718913http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30718913
http://purl.uniprot.org/citations/30718913http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30718913
http://purl.uniprot.org/uniprot/#_A4FU65-mappedCitation-30718913http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30718913
http://purl.uniprot.org/uniprot/#_B7Z8J4-mappedCitation-30718913http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30718913
http://purl.uniprot.org/uniprot/#_Q13131-mappedCitation-30718913http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30718913
http://purl.uniprot.org/uniprot/#_P30419-mappedCitation-30718913http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30718913