https://scholars.lib.ntu.edu.tw/handle/123456789/160847
Title: | SUMOYLATION ATTENUATES C-MAF-DEPENDENT IL-4 EXPRESSION | Authors: | LIN, BO-SHIOU TSAI, PEI-YUN HSIEH, WAN-YUN TSAO, HSIAO-WEI LIU, MENG-WEI WANG, LI-FANG MIAW, SHI-CHUEN 林伯修 蔡佩芸 謝婉云 曹孝瑋 劉夢薇 王莉芳 繆希椿 |
Issue Date: | Jan-2010 | Journal Volume: | 40 | Journal Issue: | 4 | Start page/Pages: | 1174-1184 | Source: | EUROPEAN JOURNAL OF IMMUNOLOGY | Abstract: | The function of transcription factors can be critically regulated by SUMOylation. c-Maf, the cellular counterpart of v-maf oncogene, is a potent transactivator of the IL-4 gene in Th2 cells. We found in a yeast two-hybrid screen that c- Maf can interact with Ubc9 and PIAS1, two key enzymes of the SUMOylation pathway. In this study, we report that c-Maf co-localized with these two SUMO (small ubiquitin-like modifier) ligases in the nucleus and that c-Maf can be SUMOylated in vitro and also in primary Th2 cells. We also demonstrated that lysine-33 is the dominant, if not the only , SUMO acceptor site of c-Maf. SUMOylation of c-Maf attenuated its transcriptional activity. Reciprocally, a SUMOylation resistant c-Maf was more potent than WT-c-Maf in driving IL-4 production in c-Maf-deficient Th2 cells. Furthermore, we showed that ablation of the SUMO site did not alter the subcellular localization or the stability of c -Maf protein but instead enhanced its recruitment to the I14 -promoter. We conclude that SUMOylation at lysine-33 is a functionally critical post-translational modification event of c-Maf in Th cells. |
URI: | http://ntur.lib.ntu.edu.tw//handle/246246/233060 |
Appears in Collections: | 免疫學研究所 |
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SUMOylation-c Maf-EJI-2010.pdf | 488.89 kB | Adobe PDF | View/Open |
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