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http://purl.uniprot.org/citations/28011284http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28011284http://www.w3.org/2000/01/rdf-schema#comment"Posttranslational modifications of certain stress granule (SG) proteins are closely related to the assembly of SGs, a type of cytoplasmic foci structure. Our previous studies revealed that the Tudor staphylococcal nuclease (Tudor-SN) protein participates in the formation of SGs. However, the functional significance of potential Tudor-SN modifications during stress has not been reported. In this study, we demonstrated that the Tudor-SN protein was phosphorylated at threonine 103 (T103) upon stimulation with arsenite. In addition, c-Jun N-terminal kinase (JNK) was found to be responsible for Tudor-SN phosphorylation at the T103 site. We further illustrated that either a T103A mutation or the suppression of phosphorylation of T103 by the JNK inhibitor SP600125 inhibited the efficient recruitment of Tudor-SN into SGs. In addition, the T103A mutation could affect the physical binding of Tudor-SN with the G3BP (Ras-GAP SH3 domain-binding protein) protein but not with the HuR (Hu antigen R) protein and AGTR1-3'UTR (3'-untranslated region of angiotensin II receptor, type 1) mRNA cargo. These data suggested that JNK-enhanced Tudor-SN phosphorylation promotes the interaction between Tudor-SN and G3BP and facilitates the efficient recruitment of Tudor-SN into SGs under conditions of sodium arsenite-induced oxidative stress. This finding provides novel insights into the physiological function of Tudor-SN modification."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.org/dc/terms/identifier"doi:10.1016/j.bbamcr.2016.12.018"xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Cui X."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Gao X."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Li L."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Ren Y."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Yang J."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Yang X."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Zhang C."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Zhao Y."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Yang W."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Su C."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Fu X."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Wei M."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Shui W."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/author"Xin L."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/name"Biochim Biophys Acta Mol Cell Res"xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/pages"562-571"xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/title"Phosphorylation of Tudor-SN, a novel substrate of JNK, is involved in the efficient recruitment of Tudor-SN into stress granules."xsd:string
http://purl.uniprot.org/citations/28011284http://purl.uniprot.org/core/volume"1864"xsd:string
http://purl.uniprot.org/citations/28011284http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28011284
http://purl.uniprot.org/citations/28011284http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28011284
http://purl.uniprot.org/uniprot/#_A0A140VK49-mappedCitation-28011284http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28011284