請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/7867完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 胡孟君 | |
| dc.contributor.author | Wen-Ting Tseng | en |
| dc.contributor.author | 曾文婷 | zh_TW |
| dc.date.accessioned | 2021-05-19T17:56:35Z | - |
| dc.date.available | 2026-12-31 | |
| dc.date.available | 2021-05-19T17:56:35Z | - |
| dc.date.copyright | 2016-08-26 | |
| dc.date.issued | 2016 | |
| dc.date.submitted | 2016-08-18 | |
| dc.identifier.citation | Amemiya Y, Azmi P, Seth A. 2008. Autoubiquitination of BCA2 RING E3 ligase regulates its own stability and affects cell migration. Molecular cancer research : MCR 6: 1385-1396.
Annicotte JS, Fayard E, Swift GH, Selander L, Edlund H, Tanaka T, Kodama T, Schoonjans K, Auwerx J. 2003. Pancreatic-duodenal homeobox 1 regulates expression of liver receptor homolog 1 during pancreas development. Mol Cell Biol 23: 6713-6724. Ashida H, Kim M, Schmidt-Supprian M, Ma A, Ogawa M, Sasakawa C. 2010. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Nat Cell Biol 12: 66-73; sup pp 61-69. Bacopulos S, Amemiya Y, Yang W, Zubovits J, Burger A, Yaffe M, Seth AK. 2012. Effects of partner proteins on BCA2 RING ligase activity. BMC cancer 12: 63. Benod C, Vinogradova MV, Jouravel N, Kim GE, Fletterick RJ, Sablin EP. 2011. Nuclear receptor liver receptor homologue 1 (LRH-1) regulates pancreatic cancer cell growth and proliferation. Proc Natl Acad Sci U S A 108: 16927-16931. Bhoj VG, Chen ZJ. 2009. Ubiquitylation in innate and adaptive immunity. Nature 458: 430-437. Bieche I, Champeme MH, Lidereau R. 1995. Loss and gain of distinct regions of chromosome 1q in primary breast cancer. Clinical cancer research : an official journal of the American Association for Cancer Research 1: 123-127. Buac D, Kona FR, Seth AK, Dou QP. 2013. Regulation of metformin response by breast cancer associated gene 2. Neoplasia 15: 1379-1390. Burger AM, Gao Y, Amemiya Y, Kahn HJ, Kitching R, Yang Y, Sun P, Narod SA, Hanna WM, Seth AK. 2005. A novel RING-type ubiquitin ligase breast cancer-associated gene 2 correlates with outcome in invasive breast cancer. Cancer Res 65: 10401-10412. Carling D, Hardie DG. 1989. The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase. Biochim Biophys Acta 1012: 81-86. Chalkiadaki A, Talianidis I. 2005. SUMO-dependent compartmentalization in promyelocytic leukemia protein nuclear bodies prevents the access of LRH-1 to chromatin. Mol Cell Biol 25: 5095-5105. Chand AL, Herridge KA, Thompson EW, Clyne CD. 2010. The orphan nuclear receptor LRH-1 promotes breast cancer motility and invasion. Endocr Relat Cancer 17: 965-975. Chau V, Tobias JW, Bachmair A, Marriott D, Ecker DJ, Gonda DK, Varshavsky A. 1989. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243: 1576-1583. Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ. 2002. Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase. J Biol Chem 277: 22085-22092. Clyne CD, Speed CJ, Zhou J, Simpson ER. 2002. Liver receptor homologue-1 (LRH-1) regulates expression of aromatase in preadipocytes. J Biol Chem 277: 20591-20597. del Castillo-Olivares A, Gil G. 2000. Alpha 1-fetoprotein transcription factor is required for the expression of sterol 12alpha -hydroxylase, the specific enzyme for cholic acid synthesis. Potential role in the bile acid-mediated regulation of gene transcription. J Biol Chem 275: 17793-17799. Dolezelova P, Cetkovska K, Vousden KH, Uldrijan S. 2012. Mutational analysis of Mdm2 C-terminal tail suggests an evolutionarily conserved role of its length in Mdm2 activity toward p53 and indicates structural differences between Mdm2 homodimers and Mdm2/MdmX heterodimers. Cell Cycle 11: 953-962. Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM. 2000. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J Biol Chem 275: 8945-8951. Fayard E, Auwerx J, Schoonjans K. 2004. LRH-1: an orphan nuclear receptor involved in development, metabolism and steroidogenesis. Trends Cell Biol 14: 250-260. Francis GA, Fayard E, Picard F, Auwerx J. 2003. Nuclear receptors and the control of metabolism. Annu Rev Physiol 65: 261-311. Giguere V. 1999. Orphan nuclear receptors: from gene to function. Endocr Rev 20: 689-725. Glickman MH, Ciechanover A. 2002. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82: 373-428. Goodwin B, Jones SA, Price RR, Watson MA, McKee DD, Moore LB, Galardi C, Wilson JG, Lewis MC, Roth ME et al. 2000. A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis. Mol Cell 6: 517-526. Gu P, Goodwin B, Chung AC, Xu X, Wheeler DA, Price RR, Galardi C, Peng L, Latour AM, Koller BH et al. 2005. Orphan nuclear receptor LRH-1 is required to maintain Oct4 expression at the epiblast stage of embryonic development. Mol Cell Biol 25: 3492-3505. Hawley SA, Boudeau J, Reid JL, Mustard KJ, Udd L, Makela TP, Alessi DR, Hardie DG. 2003. Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J Biol 2: 28. Hawley SA, Davison M, Woods A, Davies SP, Beri RK, Carling D, Hardie DG. 1996. Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J Biol Chem 271: 27879-27887. Heng JC, Feng B, Han J, Jiang J, Kraus P, Ng JH, Orlov YL, Huss M, Yang L, Lufkin T et al. 2010. The nuclear receptor Nr5a2 can replace Oct4 in the reprogramming of murine somatic cells to pluripotent cells. Cell Stem Cell 6: 167-174. Hicke L. 2001. Protein regulation by monoubiquitin. Nat Rev Mol Cell Biol 2: 195-201. Hinshelwood MM, Repa JJ, Shelton JM, Richardson JA, Mangelsdorf DJ, Mendelson CR. 2003. Expression of LRH-1 and SF-1 in the mouse ovary: localization in different cell types correlates with differing function. Mol Cell Endocrinol 207: 39-45. Honda R, Yasuda H. 2000. Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene 19: 1473-1476. Hou Y, Gao J, Xu H, Xu Y, Zhang Z, Xu Q, Zhang C. 2014. PPARgamma E3 ubiquitin ligase regulates MUC1-C oncoprotein stability. Oncogene 33: 5619-5625. Hou Y, Moreau F, Chadee K. 2012. PPARgamma is an E3 ligase that induces the degradation of NFkappaB/p65. Nature communications 3: 1300. Johansson L, Thomsen JS, Damdimopoulos AE, Spyrou G, Gustafsson JA, Treuter E. 1999. The orphan nuclear receptor SHP inhibits agonist-dependent transcriptional activity of estrogen receptors ERalpha and ERbeta. J Biol Chem 274: 345-353. Kravtsova-Ivantsiv Y, Ciechanover A. 2012. Non-canonical ubiquitin-based signals for proteasomal degradation. J Cell Sci 125: 539-548. Lai Z, Yang T, Kim YB, Sielecki TM, Diamond MA, Strack P, Rolfe M, Caligiuri M, Benfield PA, Auger KR et al. 2002. Differentiation of Hdm2-mediated p53 ubiquitination and Hdm2 autoubiquitination activity by small molecular weight inhibitors. Proc Natl Acad Sci U S A 99: 14734-14739. Lee MB, Lebedeva LA, Suzawa M, Wadekar SA, Desclozeaux M, Ingraham HA. 2005. The DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification. Mol Cell Biol 25: 1879-1890. Lee YK, Choi YH, Chua S, Park YJ, Moore DD. 2006. Phosphorylation of the hinge domain of the nuclear hormone receptor LRH-1 stimulates transactivation. J Biol Chem 281: 7850-7855. Lee YK, Parker KL, Choi HS, Moore DD. 1999. Activation of the promoter of the orphan receptor SHP by orphan receptors that bind DNA as monomers. J Biol Chem 274: 20869-20873. Lee YS, Chanda D, Sim J, Park YY, Choi HS. 2007. Structure and function of the atypical orphan nuclear receptor small heterodimer partner. Int Rev Cytol 261: 117-158. Li W, Bengtson MH, Ulbrich A, Matsuda A, Reddy VA, Orth A, Chanda SK, Batalov S, Joazeiro CA. 2008. Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling. PLoS One 3: e1487. Liu DL, Liu WZ, Li QL, Wang HM, Qian D, Treuter E, Zhu C. 2003. Expression and functional analysis of liver receptor homologue 1 as a potential steroidogenic factor in rat ovary. Biol Reprod 69: 508-517. Lu TT, Makishima M, Repa JJ, Schoonjans K, Kerr TA, Auwerx J, Mangelsdorf DJ. 2000. Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors. Mol Cell 6: 507-515. Luo Y, Liang CP, Tall AR. 2001. The orphan nuclear receptor LRH-1 potentiates the sterol-mediated induction of the human CETP gene by liver X receptor. J Biol Chem 276: 24767-24773. Matulis CK, Mayo KE. 2012. The LIM domain protein FHL2 interacts with the NR5A family of nuclear receptors and CREB to activate the inhibin-alpha subunit gene in ovarian granulosa cells. Molecular endocrinology (Baltimore, Md) 26: 1278-1290. Mrosek N, Meissburger B, Mataki C, Roeder E, Ukropec J, Klimes I, Gasperikova D, Nawroth PP, Rudofsky G, Auwerx J et al. 2013. Transcriptional regulation of adipocyte formation by the liver receptor homologue 1 (Lrh1)-Small hetero-dimerization partner (Shp) network. Mol Metab 2: 314-323. Mukhopadhyay D, Riezman H. 2007. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 315: 201-205. Nakamura N. 2011. The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function. Membranes (Basel) 1: 354-393. Nitta M, Ku S, Brown C, Okamoto AY, Shan B. 1999. CPF: an orphan nuclear receptor that regulates liver-specific expression of the human cholesterol 7alpha-hydroxylase gene. Proc Natl Acad Sci U S A 96: 6660-6665. Nityanandam R, Serra-Moreno R. 2014. BCA2/Rabring7 targets HIV-1 Gag for lysosomal degradation in a tetherin-independent manner. PLoS Pathog 10: e1004151. Ohtake F, Baba A, Takada I, Okada M, Iwasaki K, Miki H, Takahashi S, Kouzmenko A, Nohara K, Chiba T et al. 2007. Dioxin receptor is a ligand-dependent E3 ubiquitin ligase. Nature 446: 562-566. Pare JF, Roy S, Galarneau L, Belanger L. 2001. The mouse fetoprotein transcription factor (FTF) gene promoter is regulated by three GATA elements with tandem E box and Nkx motifs, and FTF in turn activates the Hnf3beta, Hnf4alpha, and Hnf1alpha gene promoters. J Biol Chem 276: 13136-13144. Peng N, Kim JW, Rainey WE, Carr BR, Attia GR. 2003. The role of the orphan nuclear receptor, liver receptor homologue-1, in the regulation of human corpus luteum 3beta-hydroxysteroid dehydrogenase type II. J Clin Endocrinol Metab 88: 6020-6028. Pezzi V, Sirianni R, Chimento A, Maggiolini M, Bourguiba S, Delalande C, Carreau S, Andò S, Simpson ER, Clyne CD. 2004. Differential Expression of Steroidogenic Factor-1/Adrenal 4 Binding Protein and Liver Receptor Homolog-1 (LRH-1)/Fetoprotein Transcription Factor in the Rat Testis: LRH-1 as a Potential Regulator of Testicular Aromatase Expression. Endocrinology 145: 2186-2196. Pollak MN. 2012. Investigating metformin for cancer prevention and treatment: the end of the beginning. Cancer Discov 2: 778-790. Rausa FM, Galarneau L, Belanger L, Costa RH. 1999. The nuclear receptor fetoprotein transcription factor is coexpressed with its target gene HNF-3beta in the developing murine liver, intestine and pancreas. Mech Dev 89: 185-188. Rennstam K, Ahlstedt-Soini M, Baldetorp B, Bendahl P-O, Borg Å, Karhu R, Tanner M, Tirkkonen M, Isola J. 2003. Patterns of Chromosomal Imbalances Defines Subgroups of Breast Cancer with Distinct Clinical Features and Prognosis. A Study of 305 Tumors by Comparative Genomic Hybridization. Cancer Research 63: 8861-8868. Rotin D, Kumar S. 2009. Physiological functions of the HECT family of ubiquitin ligases. Nat Rev Mol Cell Biol 10: 398-409. Sablin EP, Krylova IN, Fletterick RJ, Ingraham HA. 2003. Structural basis for ligand-independent activation of the orphan nuclear receptor LRH-1. Mol Cell 11: 1575-1585. Schoonjans K, Annicotte JS, Huby T, Botrugno OA, Fayard E, Ueda Y, Chapman J, Auwerx J. 2002. Liver receptor homolog 1 controls the expression of the scavenger receptor class B type I. EMBO Rep 3: 1181-1187. Seol W, Choi HS, Moore DD. 1996. An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors. Science 272: 1336-1339. Sirianni R, Seely JB, Attia G, Stocco DM, Carr BR, Pezzi V, Rainey WE. 2002. Liver receptor homologue-1 is expressed in human steroidogenic tissues and activates transcription of genes encoding steroidogenic enzymes. The Journal of endocrinology 174: R13-17. Spence J, Sadis S, Haas AL, Finley D. 1995. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol 15: 1265-1273. Stommel JM, Wahl GM. 2004. Accelerated MDM2 auto-degradation induced by DNA-damage kinases is required for p53 activation. EMBO J 23: 1547-1556. Thrower JS, Hoffman L, Rechsteiner M, Pickart CM. 2000. Recognition of the polyubiquitin proteolytic signal. EMBO J 19: 94-102. Tollini LA, Jin A, Park J, Zhang Y. 2014. Regulation of p53 by Mdm2 E3 ligase function is dispensable in embryogenesis and development, but essential in response to DNA damage. Cancer Cell 26: 235-247. Ueda H, Sun GC, Murata T, Hirose S. 1992. A novel DNA-binding motif abuts the zinc finger domain of insect nuclear hormone receptor FTZ-F1 and mouse embryonal long terminal repeat-binding protein. Mol Cell Biol 12: 5667-5672. Venteclef N, Jakobsson T, Ehrlund A, Damdimopoulos A, Mikkonen L, Ellis E, Nilsson LM, Parini P, Janne OA, Gustafsson JA et al. 2010. GPS2-dependent corepressor/SUMO pathways govern anti-inflammatory actions of LRH-1 and LXRbeta in the hepatic acute phase response. Genes Dev 24: 381-395. Wang Z, Nie Z, Chen W, Zhou Z, Kong Q, Seth AK, Liu R, Chen C. 2013. RNF115/BCA2 E3 ubiquitin ligase promotes breast cancer cell proliferation through targeting p21Waf1/Cip1 for ubiquitin-mediated degradation. Neoplasia 15: 1028-1035. Wang ZN, Bassett M, Rainey WE. 2001. Liver receptor homologue-1 is expressed in the adrenal and can regulate transcription of 11 beta-hydroxylase. Journal of molecular endocrinology 27: 255-258. Yang FM, Feng SJ, Lai TC, Hu MC. 2015. A calreticulin-dependent nuclear export signal is involved in the regulation of liver receptor homologue-1 protein folding. Biochem J 471: 199-209. Yang FM, Lin YC, Hu MC. 2011. Identification of two functional nuclear localization signals mediating nuclear import of liver receptor homologue-1. Cell Mol Life Sci 68: 1241-1253. Yang FM, Pan CT, Tsai HM, Chiu TW, Wu ML, Hu MC. 2009. Liver receptor homolog-1 localization in the nuclear body is regulated by sumoylation and cAMP signaling in rat granulosa cells. FEBS J 276: 425-436. Yang Y, Fang S, Jensen JP, Weissman AM, Ashwell JD. 2000. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288: 874-877. Zhang C, Large MJ, Duggavathi R, DeMayo FJ, Lydon JP, Schoonjans K, Kovanci E, Murphy BD. 2013. Liver receptor homolog-1 is essential for pregnancy. Nat Med 19: 1061-1066. 王志宏. 2008. mLRH-1結構功能之探討：PIASy作用區、Hinge結構區及核定位訊號. in Graduate institute of physiology, National Taiwan University. 王裕方. 2015. 探討CDK9調控核受器LRH-1的分子機制. in Graduate institute of physiology, National Taiwan University. 吳美伶. 2006. LRH-1轉錄活性調控之研究. in Graduate institute of physiology, National Taiwan University. 孟柔吟. 2015. LRH-1調控RNF138蛋白質穩定性. in Graduate institute of physiology, National Taiwan University. 許閔茹. 2013. 利用酵母菌雙雜交技術找尋在小鼠肝中與LRH-1有交互作用的蛋白質. in Graduate institute of physiology, National Taiwan University. 黃守賢. 2010. mLRH-1泛素化作用之探討. in Graduate institute of physiology, National Taiwan University. 賴財春. 2011. LRH-1離胺酸329參與泛素-蛋白酶體依賴之蛋白質水解路徑. in Graduate institute of physiology, National Taiwan University. 戴予辰. 2008. PIASγ抑制人類腎上腺細胞類固醇荷爾蒙生成基因的表現. in Graduate institute of physiology, National Taiwan University. 謝祥燦. 2007. LRH-1特性及其轉錄活性受PIASy調控之研究. in Graduate institute of physiology, National Taiwan University. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/7867 | - |
| dc.description.abstract | Liver receptor homolog-1（LRH-1, NR5A2）為一種孤兒核受器，主要表現於肝臟、小腸以及卵巢中。另外，LRH-1也是一個轉錄因子，調控許多和細胞生長、代謝以及固醇類荷爾蒙生成有關的基因。除此之外，LRH-1也參與癌細胞增生轉移的調控。RING finger protein 115（RNF115）為一種E3泛素連接酶，藉由其結構上的RING區段將目標物質接上泛素，進行泛素化作用。作為RING type的E3連接酶，它也具有將自身泛素化而降解的調控能力。
在本論文中，透過GST pull sown的實驗我們發現，RNF115與LRH-1上的DNA biding domain ( DBD ) 以及Ligand binding domain ( LBD ) 具有交互作用。當RNF115和LRH-1同時轉染於HEK293T細胞中，LRH-1蛋白質量並沒有降低的情形；相反的，RNF115卻顯著降低。隨著LRH-1劑量增加，RNF115被抑制的程度亦隨之增加。另外，利用蛋白質衰減測定，我們發現LRH-1會降低RNF115蛋白質的穩定性。若在我們給予MG132處理後，LRH-1對RNF115蛋白質量的減少作用有顯著性的減緩。此結果說明，蛋白酶體系統降解路徑對於LRH-1調控RNF115扮演相當重要的角色。先前的文獻指出，核受器的DBD區域可能潛在有RING finger的結構。將LRH-1 DBD片段剔除後，對RNF115作用顯著降低。另外將位於LRH-1 DBD鋅指結構上幾個重要位點進行突變後，LRH-1失去轉錄活性，而RNF115蛋白質量的減少大幅減緩。除此之外，LRH-1中LBD片段剔除以及將LBD上AF-2區域與輔助因子連接的重要位點突變後，RNF115的量顯著恢復。綜合結果顯示，LRH-1主要經由泛素-蛋白酶體路徑促進RNF115的降解，而LRH-1中的DBD與LBD在此調控中可能扮演著相當重要的角色。 | zh_TW |
| dc.description.abstract | Liver receptor homolog-1 (LRH-1, NR5A2), an orphan nuclear receptor, is mainly expressed in liver, intestine and ovary. LRH-1 is a transcription factor and regulates the expression of genes involved in development, metabolism and steroidogenesis. In addition, LRH-1 is implicated in several cancers. RING finger protein 115（RNF115）is an E3 ubiquitin ligase that contains a RING domain to help the conjugation of ubiquitin to the substrate proteins including itself.
In this study, we performed GST-pull down experiments to show that LRH-1 interacted with RNF115 through DNA binding domain（DBD）and ligand binding domain (LBD). When co-transfected with RNF115 in HEK293T cells, the level of LRH-1 protein was not altered. In contrast, we found that the protein level of RNF115 dramatically reduced in the presence of LRH-1. The cycloheximide-based pulse-chase assays revealed that LRH-1 reduced the protein stability of RNF115. Treatment with proteasome inhibitor MG132, but not lysosomal inhibitor, significantly attenuated the inhibitory effects of LRH-1 on RNF115 protein levels. The data suggested that LRH-1 promotes the degradation of RNF115through proteasome system. Recent studies indicated that the DBD of nuclear receptor PPARγ has the potential to form RING finger-like structure and possess the E3 ubiquitin ligase activity. We found that truncated LRH-1with DBD deletion attenuated the inhibitory effects of LRH-1 on RNF115 protein levels. Experiment with LRH-1 mutants showed that the zinc finger region in DBD, but not the transcriptional activity, was important for LRH-1-induced RNF115 degradation. The AF-2 in LBD is an important region for the interaction between LRH-1 and coregulators. LBD deletion or AF-2 mutation decreased LRH-1-induced RNF115 degradation.Our results suggested LRH-1 negatively regulates RNF115 protein stability through ubiquitin proteasome degradation pathway and the DBD and LBD of LRH-1 may play some roles in this process. | en |
| dc.description.provenance | Made available in DSpace on 2021-05-19T17:56:35Z (GMT). No. of bitstreams: 1 ntu-105-R03441013-1.pdf: 2523247 bytes, checksum: dd41ba52634a3355d2f05080f978bbae (MD5) Previous issue date: 2016 | en |
| dc.description.tableofcontents | 目錄 III
圖次 V 中文摘要 VI Abstract VII 第一章 序論 1 一、 LRH-1簡介 1 1. LRH-1之蛋白質結構 1 2. LRH-1之生理功能 1 3. LRH-1之轉譯後修飾作用 4 二、 泛素（ubiquitin）-蛋白酶體（proteasome）系統 5 1. 泛素修飾之作用機轉 5 2. 泛素鍵結結構種類功能 5 三、 RNF115簡介 6 1. RNF115蛋白質結構 6 2. RNF115之作用 7 四、 研究目的 9 第二章 材料與方法 10 一、 細胞培養 10 二、 質體 10 三、 暫時性轉染法（Transient transfection） 18 四、 質體點突變（Mutagenesis） 19 五、 西方墨點法（Western blot）分析 19 六、 冷光酶活性分析（Luciferase assay） 21 七、 免疫沉澱法（Immunoprecipitation） 21 八、 GST沉澱法（GST pull-down） 23 九、 免疫螢光染色法（Immunofluorence） 24 十、 蛋白質半衰期（protein half-life）測定 25 第三章 結果 26 一、 LRH-1影響RNF115蛋白質的量 26 二、 LRH-1與RNF115在細胞中的分布 26 三、 LRH-1與RNF115蛋白質交互作用區域 26 四、 LRH-1影響RNF115蛋白質穩定性 27 五、 LRH-1促進RNF115蛋白質降解的路徑 27 六、 LRH-1對RNF115作用機制 29 七、 LRH-1調控RNF115重要區段分析 30 第四章 討論 32 一、 LRH-1對RNF115作用區域 32 1. 離胺酸位點 32 2. 其它位點 32 二、 LRH-1降低RNF115蛋白作用機制 33 1. 促進自我泛素化 33 2. LRH-1的轉錄活性 34 3. LRH-1具有E3連接酶活性 34 4. LRH-1藉由招募其他因子 35 參考文獻 36 | |
| dc.language.iso | zh-TW | |
| dc.title | LRH-1調控RNF115蛋白質穩定性 | zh_TW |
| dc.title | Liver receptor homolog-1 regulates the stability of RING finger protein 115 | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 104-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 張淑芬,徐立中,鄭瓊娟 | |
| dc.subject.keyword | LRH-1,RNF115,BCA2, | zh_TW |
| dc.relation.page | 55 | |
| dc.identifier.doi | 10.6342/NTU201603267 | |
| dc.rights.note | 同意授權(全球公開) | |
| dc.date.accepted | 2016-08-18 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 生理學研究所 | zh_TW |
| dc.date.embargo-lift | 2026-12-31 | - |
| 顯示於系所單位： | 生理學科所 | |
文件中的檔案：
| 檔案 | 大小 | 格式 | |
|---|---|---|---|
| ntu-105-1.pdf 此日期後於網路公開 2026-12-31 | 2.46 MB | Adobe PDF |
系統中的文件，除了特別指名其著作權條款之外，均受到著作權保護，並且保留所有的權利。