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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 周祖述 | |
dc.contributor.author | Chun-Ying Yu | en |
dc.contributor.author | 余俊頴 | zh_TW |
dc.date.accessioned | 2021-06-13T15:39:15Z | - |
dc.date.available | 2008-08-13 | |
dc.date.copyright | 2008-08-13 | |
dc.date.issued | 2008 | |
dc.date.submitted | 2008-07-09 | |
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Conference on microdomains, lipid rafts and caveolae. EMBO Rep. 4:1117-21. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/37698 | - |
dc.description.abstract | PC/Gp135近來發現參予了細胞頂部區域的形成,此功能的執行需要Gp135被正確的運送至頂部區域。我們發現Gp135藉由雙訊息的雙重保障,確保了正確的運送。此雙重訊息由Gp135蛋白上兩區域所組成,一者為細胞外富涵O型醣化修飾的區域,另一為細胞內可與PDZ結構域辨認結合的序列。我們藉由接合喪失此序列的Gp135與此序列所辨認反應的PDZ結構域蛋白(EBP50),來確認序列的功能。根據我們的觀察,EBP50在高基式體即與Gp135接合,加速Gp135的多單位體形成,一同組成運送至頂部區域的複合體。缺少序列,無法與EBP50反應的Gp135,或是剃除細胞內的EBP50,皆會造成Gp135延遲離開脂筏,無法順利組成多單位體,並且錯誤運送至MDCK細胞的側邊區域。這些錯誤運送的Gp135會藉由PKC酵素所影響的機制,快速的被細胞內噬。另一方面,我們發現了乳糖凝集素-8可與細胞外富涵O型醣修飾的區域結合,促成Gp135的多單位體形成,與中和O型醣上由唾液酸修飾所造成的負電荷,避免負電排斥力造成運送液泡的分解。與剔除EBP50的反應類似,將細胞內的乳糖凝集素-8剃除,亦能使Gp135延遲離開脂筏,並錯誤的運送至MDCK細胞的側邊區域。因此,我們提出了一種模型,說明了高負電價的膜蛋白,可藉由細胞內的接合蛋白(EBP50)與細胞外的中和接合蛋白(乳糖凝集素-8),形成運送至頂部區域的複合體,有效且正確的運送Gp135至頂部區域。此外,我們發現細胞可藉由不同的乳糖凝集素,將具有相對應醣修飾的蛋白聚集成相異的
運送液泡。藉此機制,細胞可利用醣化來控制蛋白質的運送。 | zh_TW |
dc.description.abstract | Podocalyxin (PC)/Gp135 was recently demonstrated to participate in the formation of a pre-apical complex to set up initial polarity in MDCK cells, a function presumably depending on the apical targeting of Gp135. We show that correct apical sorting of Gp135 depends on a bipartite signal composed of an extracellular O-glycosylation rich region and the intracellular PDZ domain binding motif. The function of this PDZ binding motif could be substituted with a fusion construct of Gp135 with Ezrin binding phosphoprotein 50 (EBP50). In accordance with this observation, EBP50 binds to newly synthesized Gp135 at Golgi apparatus, and facilitates oligomerization and sorting of Gp135 into clustering complex. Defective connection between Gp135 and EBP50 or EBP50 knock-down results in a delayed exit from the detergent resistant microdomain (DRM), failure of oligomerization, and basolateral missorting of Gp135. The basolaterally missorted EBP50 binding defective mutant of Gp135 was rapidly retrieved via a PKC-dependent mechanism. Moreover, we found that Galectin-8 could cluster Gp135 and neutralize the negative charges of Gp135 through interacting with extracellular O-glycosylation rich region. Knock-down of Galectin also delay the exist from DRM and causes the basolateral missorting of Gp135.According to these findings, we propose a model by which a highly negative charged transmembrane protein could be packed into an apical sorting platform with the aids of its cytoplasmic partner EBP50 and extracellular partner Galectin-8. We also found that Galectins could segregate glycoproteins into different sorting cargos. We propose that cells could direct the sorting and timing of glycoprotein by controlling the glycosylation and Galectin expression. | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T15:39:15Z (GMT). No. of bitstreams: 1 ntu-97-F92448009-1.pdf: 5905238 bytes, checksum: 47490d49692285b54e53f0a7cd6ddf1e (MD5) Previous issue date: 2008 | en |
dc.description.tableofcontents | 中文摘要 1
Abstract 3 Lecture reviews 4 1. The polarity of epithelial cells 4 2. Two pathways to transport membrane protein in epithelial cells 5 3. Signals direct basolateral protein sorting 6 4. Signals direct apical protein sorting 6 4.1 GPI anchorage and DRM 7 4.2 Glycosylations 8 4.2a N-glycosylation 9 4.2b O-glycosylation 10 4.2c The lectin receptor for glycosylation 11 4.3a The intrinsic motif in peptide chain 12 4.3b PDZ binding motif and PDZ domain containing protein EBP50 12 5. Galectins 14 5.1 Galectin-3 14 5.2 Galectin-8 15 6. The marker proteins of apical domain of MDCK cells 15 6.1 Podocalyxin (PC)/Gp135 16 6.2 CEACAM1/Gp114 17 Chapter I 18 Abstract 18 Introduction 19 Materials and Methods 21 Results 26 Both Extracellular and Intracellular Domains of Gp135 Contain Apical Targeting Signals 26 The O-Glycan Rich Region of the Extracellular Domain Contains an Apical Sorting Signal for Gp135 27 The PDZ Binding Motif in the Cytoplasmic Tail Contains an Apical Sorting Signal for Gp135 29 The Basolaterally Mis-targeted m135dC Mutant Was Rapidly Endocytosed in a PKC-dependent Manner 31 Fusion of EBP50 to the m135dC Mutant Restored the Apical Sorting Signal 33 EBP50 Binds to Newly Synthesized Gp135 34 Lipid Raft Association Is Required, but Not Sufficient, for Apical Sorting of Gp135 37 Basolaterally Missorted dN122dC Mutant Proteins Are Monomeric and Associated with Detergent Resistant Microdomain 39 EBP50 Knock-Down Results in a Failure of Oligomerization, Retention in the Lipid Raft, and Basolaterally Missorting of the Newly Synthesized Gp135/PC. 40 Discussion 43 Chapter II 47 Abstract 47 Introduction 48 Materials and Methods 51 Result 54 The Galectins expression pattern in MDCK cells 54 Galectins interacts with different membrane glycoproteins 55 Galectin-3 is localized with CEACAM1/Gp114 on the apical domain of MDCK cells. 57 Galectin-8 is localized with PC/Gp135 on microvillus. 58 Knockdown of Galectin-8 causes a failure of oligomerization and missorting of Gp135 58 Galectin-8 Binds to Newly Synthesized Gp135 59 The specific isoform of CEACAM1/Gp114, CEACAM1-I4S, is expressed on the apical domain of MDCK cells 60 The model of segregated apical sorting cargos 62 Discussion 63 References 67 Figure 76 Appendix………117 | |
dc.language.iso | en | |
dc.title | Podocalyxin/Gp135 藉雙重訊息正確運送至細胞頂域 | zh_TW |
dc.title | A bipartite signal regulates the faithful delivery of apical domain marker podocalyxin/Gp135 | en |
dc.type | Thesis | |
dc.date.schoolyear | 96-2 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 李芳仁,林奇宏,嚴仲陽,邱繼煇 | |
dc.subject.keyword | 極性,Gp135,頂部區域,蛋白質運送,乳醣凝集素,EBP50, | zh_TW |
dc.subject.keyword | GP135,apical domain,sorting,polarity,Galectin,EBP50, | en |
dc.relation.page | 116 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2008-07-09 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 分子醫學研究所 | zh_TW |
顯示於系所單位: | 分子醫學研究所 |
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