請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/18512完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 李芳仁 | |
| dc.contributor.author | Tsai-Chen Chiang | en |
| dc.contributor.author | 江采蓁 | zh_TW |
| dc.date.accessioned | 2021-06-08T01:09:08Z | - |
| dc.date.copyright | 2014-10-09 | |
| dc.date.issued | 2014 | |
| dc.date.submitted | 2014-08-18 | |
| dc.identifier.citation | Reference
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/18512 | - |
| dc.description.abstract | ARL4 (ARF-Like 4) small G protein subfamily belongs to ADP-Ribosylation Factor (Komander et al.) of Ras small GTPase superfamily. ARL4 subfamily consists of ARL4A, ARL4C and ARL4D. Transient expression patterns of ARL4s have been reported responded to physiological conditions, such as embryonic development, tissue morphogenesis and stress. Recent studies show that ARL4s are regulators of cellular cytoskeleton and upstream of ARF6 signaling pathways. Cell migration participates in development of functional organ in embryonic development and systematic balance when adult. Coordination of multiple signaling pathways involving in cytoskeleton and membrane dynamics, cell adhesion and cell polarity are required for promoting cell migration. In this study, we explore signaling pathways of ARL4A in membrane protrusion, cell adhesion and cell migration. We found ARL4A was mainly localized at membrane through both targeting signals of N-terminal myristoylation and C-terminal polybasic motif. ARL4A promoted membrane protrusion on fibronectin and increased cell spreading in nucleotide binding dependent manner. ARL4A also induced focal adhesion dynamics. Depletion of ARL4A affected focal adhesion morphology. It implies that ARL4A plays a role in cell migration. Our previous study shows that ELMO is ARL4A interacting protein. Interaction of ELMO with ARL4A through N-terminal Ras-binding domain (RBD) affects ARL4A-induced cell spreading and actin remodeling. Here, we identify p21-activating kinase (PAK) as novel interacting protein of ARL4A. Similar to ELMO-RBD interaction, ARL4A interacted with PAK through p21-binding domain (PBD), which is required for active Cdc42 and Rac1 binding. Expression of ARL4A promoted PAK/β-PIX /GIT1 complexes to membrane protrusion. Disruption β-PIX interaction and depletion PAK1 diminished ARL4A-induced membrane protrusion. Moreover, we found that residues R105 and K114 in the C-terminal PBD domain were required for ARL4A and PAK interaction. Replacement of R105 and K114 to alanine abolished ARL4A interaction and cell migration. Taken together, in this study, we reveal ARL4A function in membrane protrusion, cell adhesion and cell migration through interaction with PAK in integrin-mediated signaling pathway. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-08T01:09:08Z (GMT). No. of bitstreams: 1 ntu-103-D96448010-1.pdf: 10803771 bytes, checksum: 6b3633a252b3fb4854f9a6776df9efa0 (MD5) Previous issue date: 2014 | en |
| dc.description.tableofcontents | Table of Contents
Table of Contents………………………………………………….................................………………..…….1 中文摘要 ……..……………………………………………….….…………………………..……..……..………4 Abstract…….………………………..……………………………………………………….……..….....………...5 Introduction 1. Small GTPases ……….………………………………...………………………………………….……….7 2. ADP-ribosylation factor family……...…………………......…………….……...…...……………….7 3. ARL4 (ADP-ribosylation factor-like 4) subfamily GTPases……………...…...…..……...10 4. The specificity of ARL4A 4.1. Transcriptional regulation……………………...……………..………………………...………11 4.2. Signaling for induction of ARL4A expression…………………………..………..……..12 5. ARL4 interaction protein 5.1. Importin-α ……………...…………..……………………...….....………….………………………13 5.2. ARF-GEF Cytohesin……………...………….…………………………………………………...13 5.3. Golgin GCC185…………………...………………………………….…………………………….14 6. Cell migration………………………..…………………………….………………………………….......14 7. ELMO/DOCK180 complex 7.1. Introduction…………...…………………………..………………………………………………….15 7.2. Protein structure of ELMO family………..………………….…….………………………...16 7.3. ELMO/DOCK180 complex in cell migration…………….….…….………..……….…..16 8. p21-activating protein (PAK) 8.1. Introduction ………………………....………………………………………………………………17 8.2. Protein structure of group I PAK……………………………………………...……………...17 8.3. Mechanism of group I PAK activation …………...…………….…………..……..…..…..18 8.4. Localization of group I PAK…………………………………………………..….……...…….19 8.5. p21-activating protein in cell migration…………………………...….…………..….....….20 8.6. p21-activating protein in focal adhesion dynamics ……………….........…………..….21 Materials and Methods……………………...………………...……………………………….…………….23 Results………………………………………...……………………..…………………………….……………...34 Discussion…………………………………………………..…...….………...………………….………….......47 Figures Figure 1: Localization of ARL4 family small GTPases. ……………..………………….………55 Figure 2: Cell spreading area decreases in ARL4A siRNA treated cells. ………..……......56 Figure 3: ARL4A induces membrane protrusion when cell spreading on fibronectin. ………………………………………………………………………………..................…….……………...……..57 Figure 4: The subcellular localization of ARL4A in cells spreading on fibronectin. …………………..………………………………………………………......................................58 Figure 5: Expression of active ARL4A affects focal adhesions. ………..…………..…...…...59 Figure 6: ARL4 expression affects focal adhesion morphology. ………………..…..……….60 Figure 7: Expression of ARL4A in human cancer cell lines……………………………………61 Figure 8: ARL4A is upregulated in cervical cancer cell C33A……………………………...…62 Figure 9: ARL4A and ARL4D are degraded after blockage of protein synthesis by cycloheximide…………………………………..………………………………………………………..…......63 Figure 10: Exogenous and endogenous ARL4A localize at membrane-enriched fractions…………………………………………………………………….…………………………….….……64 Figure 11: ARL4A depletion affects paxillin distribution. …………………..…………….……65 Figure 12: ARL4A is required for cell trans-migration toward fibronectin…………….….66 Figure 13: Overexpression of ARL4A promotes cell trans-migration toward fibronectin…..………………………………………………………………………………………….……..….67 Figure 14: ARL4A interacts with PAK p21-binding domain (PAK-PBD). ………..….….68 Figure 15: Mapping of the interaction region of ARL4A with PAK1. ..……………...........69 Figure 16: Active form of ARL4A interacts with PAK-PBD. ……………………………...…70 Figure 17: Different binding properties of ARL4A and Rac1 to PAK1…………………….71 Figure 18: Rac1 interaction with PAK-PBD in the presence of ARL4A in vitro.......…72 Figure 19: Identification of ARL4A-binding sites in PAK-PBD. ………………………..…...73 Figure 20: ARL4A-PAK1 interaction in vivo. …………………………………………………...…74 Figure 21: Nucleotide-binding defect of ARL4A does not enrich PAK1 to membrane protrusion. ……………………………………………………………………………………………………….75 Figure 22: ARL4A is co-localized with PAK1, b-PIX and GIT1 at ARL4A-induced membrane protrusion. ………………………………………………………………………………….……76 Figure 23: PAK1 deficient in b-Pix binding fails to be recruited to membrane by ARL4A. ……………………………………………………….……………………………………………….…77 Figure 24: PAK1 mutant deficient in ARL4A binding affects cell migration. ……….….78 Figure 25: Depletions of PAK1 and PAK2 show distinct effects in ARL4A-induced membrane protrusion. ………………………………………………………………...................................79 Reference …………………………………………...……………………………...……………………..…..…81 | |
| dc.language.iso | en | |
| dc.title | 探討腺嘌呤核苷二磷酸核醣化因子相似蛋白四 A之功能 | zh_TW |
| dc.title | Functional Characterization of ADP-Ribosylation
Factor-Like Protein 4A (ARL4A) | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 102-2 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 陳瑞華,張智芬,陳鴻震,周祖述 | |
| dc.subject.keyword | 鳥糞嘌呤核?三磷酸?,腺嘌呤核?二磷酸核醣化因子,腺嘌呤核?二磷酸核醣化因子相似蛋白四 A, | zh_TW |
| dc.subject.keyword | small GTPases,ADP-ribosylation factor,ARL4, | en |
| dc.relation.page | 90 | |
| dc.rights.note | 未授權 | |
| dc.date.accepted | 2014-08-18 | |
| 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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