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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 繆希椿 | |
| dc.contributor.author | Bo-Shiou Lin | en |
| dc.contributor.author | 林伯修 | zh_TW |
| dc.date.accessioned | 2021-05-20T21:34:38Z | - |
| dc.date.available | 2012-09-09 | |
| dc.date.available | 2021-05-20T21:34:38Z | - |
| dc.date.copyright | 2010-09-09 | |
| dc.date.issued | 2010 | |
| dc.date.submitted | 2010-08-17 | |
| dc.identifier.citation | Bauquet, A.T., Jin, H., Paterson, A.M., Mitsdoerffer, M., Ho, I.C., Sharpe, A.H., and Kuchroo, V.K. (2009). The costimulatory molecule ICOS regulates the expression of c-Maf and IL-21 in the development of follicular T helper cells and TH-17 cells. Nature immunology 10, 167-175.
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/10502 | - |
| dc.description.abstract | 轉錄因子的功能是藉由控制其生成、活性與降解來嚴格調控的，而SUMO化修飾是在轉錄後層級調控蛋白質的活性。c-Maf蛋白是屬於大Maf家族的鹼性白氨酸拉鍊蛋白，在第二或第十七型輔助T細胞上分別為介白素四與介白素二十一的專一性轉錄因子。我們藉由酵母雙雜交系統來尋找c-Maf的交互作用蛋白。我們發現兩個SUMO化修飾的關鍵酵素：Ubc9與PIAS1，可以與c-Maf蛋白交互作用。在T細胞中，PIAS1可以與c-Maf蛋白交互作用；這兩個SUMO化修飾的關鍵酵素也與c-Maf蛋白共同位於細胞核中。我們也確認c-Maf蛋白在活體外與活體內都可被SUMO修飾。c-Maf蛋白N端第33個離胺酸是SUMO蛋白的修飾位。SUMO化修飾會降低c-Maf蛋白對介白素四的轉錄活性，而無法被SUMO化修飾的c-Maf蛋白卻有較強的轉錄活性。同時，我們也發現c-Maf是介白素二十一的專一性轉錄因子。SUMO化修飾也會影響c-Maf蛋白相關之介白素二十一的產生。SUMO化修飾不會影響c-Maf蛋白的穩定性，但無法SUMO化修飾的c-Maf蛋白匯集到啟動子的能力卻較強。我們的結論是c-Maf蛋白的SUMO化修飾對其在輔助T細胞中的活性十分重要。 | zh_TW |
| dc.description.abstract | The function of transcription factor is tightly regulated by controlling their synthesis, activity and degradation. SUMOylation modulates target protein activity on post-translational level. c-Maf, the cellular homologue of v-Maf, is a basic-leucine zipper protein and belongs to the large Maf family. In helper T cells, c-Maf is the specific transcription factor of the IL-4 and IL-21 genes in type 2 T helper (Th2) and type 17 T helper (Th17) cells, respectively. In our study, we performed the yeast two-hybrid assay to identify the c-Maf interacting proteins. We found that c-Maf can interact with Ubc9 and PIAS1, the key enzymes of SUMOylation system. In T cells, c-Maf interacts with PIAS1 in primary T cells and also co-localizes with these two SUMO ligases in the nucleus. We also demonstrated that c-Maf can be SUMOylated in vitro and also in vivo. We identified the c-Maf SUMO acceptor site(s) by mutated the putative conjugating lysine residues. We demonstrated that N-terminal lysine-33 within the activation domain is the SUMO acceptor site for c-Maf. SUMO modification attenuates Wt-c-Maf transcriptional activity. Conversely, c-Maf SUMO deficient mutant is more potent to drive IL-4 production in Th2 cells. Furthermore, we showed that c-Maf, but not other transcription factor, transactivates IL-21 gene expression. SUMOylation also affects c-Maf dependent IL-21 production. In addition, SUMO deficient c-Maf does not alter the localization and the protein stability, but further enhances its recruitment to the Il4-promoter. We conclude that post-translational lysine-33 SUMOylation is critical for c-Maf activity in helper T cells. | en |
| dc.description.provenance | Made available in DSpace on 2021-05-20T21:34:38Z (GMT). No. of bitstreams: 1 ntu-99-D91449003-1.pdf: 18093645 bytes, checksum: b0d6d37baed2615722c878023dfb7b28 (MD5) Previous issue date: 2010 | en |
| dc.description.tableofcontents | Table of contents
Table of contents…………...…..i List of Figures……………………………..……………...iv Appendix…......……..…………………..……………….....v 口試委員審定書……………...……….......vi Acknowledgement…………....vii 中文摘要……………...……….......ix Abstract……………...……….......x Chapter I Introduction……………….…...……..1 1.1 T helper cell lineages and their differentiation………………..1 1.2 Overview of c-Maf………….………………………..…..4 1.3 The functions of c-Maf in immune system……………..5 1.4 Post-translational modification by SUMOylation: a ubiquitin-like modification system……………………...……………………….…..7 1.5 Rationale and significance…………...………….……...9 Chapter II Materials and Methods……..……….……...11 Part 1. Materials………………11 2.1-1 Antibodies………………...11 2.1-2 Cell cultures and mice……...…………………...…..11 2.1-3 Chemicals and reagents……………………………..12 2.1-4 Cytokines………………12 2.1-5 kits……………………..13 2.1-6 Vectors………...……….…13 Part 2. Methods……………..…15 2.2-1 Immunoprecipitation assay……………………..…..15 2.2-2 Intracellular cytokine staining………………...….....16 2.2-3 In vitro Th cell differentiation………………......…..16 2.2-4 In vivo and In vitro SUMOylation assay……….…..17 2.2-5 Luciferase assay………………………..…………...17 2.2-6 Protein stability assay………………...……………..18 2.2-7 Quantitative real-time PCR…………………......…..18 2.2-8 Retroviral constructs and transduction……………………...………………..…..19 2.2-9 Statistical analysis…………...…………………………...……………………....19 2.2-10 Yeast two-hybrid assay…………………………….19 Chapter III Results…………………………...………….21 3.1 Screening the c-maf interacting proteins……………...21 3.2 c-Maf interacts with PIAS1 and Ubc9…………….......21 3.3 c-Maf is SUMOylated both in vitro and in vivo………....22 3.4 Lycine 33 is the dominant SUMO acceptor site of c-Maf………………………….24 3.5 SUMOylation attenuates c-Maf transactivity…………25 3.6 SUMOylation of c-Maf in Th2 clone and primary Th2 cells………………………26 3.7 SUMOylation suppresses c-Maf-dependent Il4 gene expression……......................26 3.8 DeSUMOylation enhances the recruitment of c-Maf to the Il4-promoter…………28 3.9 c-Maf, but not other transcription factors, transactivates Il-21 gene expression…...30 3.10 c-Maf indues IL-21 expression through proximal MARE site……………………31 3.11 c-Maf is SUMOylated in Th17 cells…………...….....32 3.12 SUMOylation deficient K33R c-Maf has more potent IL-21 gene transactivity…32 Chapter IV Discussions…………………………….…....34 Chapter V Figures and Tables………….……………….44 References………………....69 Appendix…………………..81 | |
| dc.language.iso | en | |
| dc.title | SUMO化修飾減弱c-Maf相關之介白素四與介白素二十ㄧ之表現 | zh_TW |
| dc.title | SUMOylation attenuates c-Maf-dependent IL-4 and IL-21 expression | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 98-2 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 謝世良,許秉寧,賴明宗,司徒惠康 | |
| dc.subject.keyword | SUMO化修飾,c-Maf蛋白, | zh_TW |
| dc.subject.keyword | SUMOylation,c-Maf, | en |
| dc.relation.page | 88 | |
| dc.rights.note | 同意授權(全球公開) | |
| dc.date.accepted | 2010-08-17 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 免疫學研究所 | zh_TW |
| 顯示於系所單位： | 免疫學研究所 | |
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