期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
卷 1864, 期 3, 页码 562-571出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2016.12.018
关键词
Tudor-SN; Stress granules; Phosphorylation; C-Jun N-terminal kinase; Stress
资金
- National Science Foundation for Distinguished Young Scholars of China [31125012]
- Innovation Team Development Plan of the Ministry of Education [IRT13085]
- NSFC [31370749, 81570256, 31571380, 31670759]
- Tianjin Research Program of Application Foundation and Advanced Technology [15JCQNJC09900]
- Canadian Institutes of Health Research [MOP-130423]
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. (C) 2016 Elsevier B.V. All rights reserved.
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