http://purl.uniprot.org/citations/28011284 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/28011284 | http://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/28011284 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbamcr.2016.12.018"xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Cui X."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Gao X."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Li L."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Ren Y."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Yang J."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Yang X."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Zhang C."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Zhao Y."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Yang W."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Su C."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Fu X."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Wei M."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Shui W."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/author | "Xin L."xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta Mol Cell Res"xsd:string |
http://purl.uniprot.org/citations/28011284 | http://purl.uniprot.org/core/pages | "562-571"xsd:string |
http://purl.uniprot.org/citations/28011284 | http://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/28011284 | http://purl.uniprot.org/core/volume | "1864"xsd:string |
http://purl.uniprot.org/citations/28011284 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/28011284 |
http://purl.uniprot.org/citations/28011284 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/28011284 |
http://purl.uniprot.org/uniprot/#_A0A140VK49-mappedCitation-28011284 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28011284 |