Phosphorylation of Tudor-SN, a novel substrate of JNK, is involved in the efficient recruitment of Tudor-SN into stress granules

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• 作者：Chao Su^a ; ^b ; ^c ; ^d ; ¹ ; Xingjie Gao^a ; ^b ; ^c ; ^d ; ¹ ; Wendong Yang^a ; ^c ; ^d ; ¹ ; Yali Zhao^a ; ^c ; ^d ; Xue Fu^a ; ^c ; ^d ; Xiaoteng Cui^a ; ^c ; ^d ; Chunyan Zhang^a ; ^c ; ^d ; Lingbiao Xin^a ; ^c ; ^d ; Yuanyuan Ren^a ; ^c ; ^d ; Lixin Li^e ; Wenqing Shui^e ; Xi Yang^f ; Minxin Wei^g ; ^{minxinw@126.com} ; Jie Yang^a ; ^b ; ^c ; ^d ; ^{yangj@tmu.edu.cn}
• 刊名：Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1864
• 期：3
• 页码：562-571
• 全文大小：1933 K
• 卷排序：1864

文摘

Tudor-SN protein was phosphorylated at T103 site upon arsenite stimulation. JNK was responsible for Tudor-SN phosphorylation at T103 site. T103 phosphorylation was linked to the efficient recruitment of Tudor-SN into SGs. T103A mutation affected the physical binding of Tudor-SN with G3BP.