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

Article ID	Journal	Published Year	Pages	File Type
5508759	Biochimica et Biophysica Acta (BBA) - Molecular Cell Research	2017	10 Pages	PDF

Keywords

Tudor-SN TTP cdc2 HRI G3BP mTORC1 PKR eIF4E GCN2 Hu antigen R SND1 eIF2α PP1 RNA-binding protein immunoprecipitation KLH Jnk eukaryotic translation initiation factor 4E c-Jun N-terminal kinase CDKs LC-MS/MS MAPK PKR-like endoplasmic reticulum kinase Stress matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Immunofluorescence ANOVA one-way analysis of variance eukaryotic translation initiation factor 2 alpha Tristetraprolin standard error Liquid chromatography-tandem mass spectrometry Phosphorylation MALDI-TOF MS Mammalian target of rapamycin complex 1 RIP protein phosphatase 1 protein kinase R mitogen activated protein kinase cyclin-dependent protein kinases PERK HuR keyhole limpet hemocyanin general control nonderepressible 2 Stress granules Stress granule

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

Authors

Chao Su, Xingjie Gao, Wendong Yang, Yali Zhao, Xue Fu, Xiaoteng Cui, Chunyan Zhang, Lingbiao Xin, Yuanyuan Ren, Lixin Li, Wenqing Shui, Xi Yang, Minxin Wei, Jie Yang,