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http://purl.uniprot.org/citations/31135971http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31135971http://www.w3.org/2000/01/rdf-schema#comment"Protein 4.1R, an 80 000 MW membrane skeleton protein, is a vital component of the red blood cell membrane cytoskeleton that stabilizes the spectrin-actin network and regulates membrane properties of deformability and mechanical stability. It has been shown that 4.1R is expressed in T cells, including CD8+ T cells, but its role in CD8+ T cells remains unclear. Here, we have explored the role of 4.1R in CD8+ T cells using 4.1R-/- mice. Our results showed that cell activation, proliferation and secretion levels of interleukin-2 and interferon-γ were significantly increased in 4.1R-/- CD8+ T cells. Furthermore, the phosphorylation levels of linker for activation of T cells (LAT) and its downstream signaling molecule extracellular signal-regulated kinase were enhanced in the absence of 4.1R. In vitro co-immunoprecipitation experiments showed a direct interaction between 4.1R and LAT. Moreover, 4.1R-/- CD8+ T cells and mice exhibited an enhanced T-cell-dependent immune response. These data enabled the identification of a negative regulation function for 4.1R in CD8+ T cells by a direct association between 4.1R and LAT, possibly through inhibiting phosphorylation of LAT and then modulating intracellular signal transduction."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.org/dc/terms/identifier"doi:10.1111/imm.13085"xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Dai L."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Fan D."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Guo Y."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Ji Z."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Liu J."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Zhang L."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Wang W."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/author"Kang Q."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/name"Immunology"xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/pages"312-321"xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/title"Protein 4.1R negatively regulates CD8+ T-cell activation by modulating phosphorylation of linker for activation of T cells."xsd:string
http://purl.uniprot.org/citations/31135971http://purl.uniprot.org/core/volume"157"xsd:string
http://purl.uniprot.org/citations/31135971http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31135971
http://purl.uniprot.org/citations/31135971http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31135971
http://purl.uniprot.org/uniprot/#_A0A0U1RP03-mappedCitation-31135971http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31135971
http://purl.uniprot.org/uniprot/#_A0A068WAQ5-mappedCitation-31135971http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31135971
http://purl.uniprot.org/uniprot/#_A0A068WAZ7-mappedCitation-31135971http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31135971