Дисертації з теми "Arl15"
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Panić, Bojana. "The small GTPases Arl1p/Arl1 and Arl3p/ARFRP1 act in a pathway for targeting proteins to the Golgi apparatus." Thesis, University of Cambridge, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.616124.
Повний текст джерелаLasić, Maja. "The yeast endosomal/TGN-localized Ysl2p-Arl1p-Neo1p network: search for novel interaction partners." [S.l. : s.n.], 2008. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-34910.
Повний текст джерелаFerreira, Cláudia Susana da Rosa. "Organelle-specific roles for the Arf-like G proteins Arl5 and Arl8." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609430.
Повний текст джерелаMan, Zhiqiu. "Localization and function of Arfaptins: Arl1-dependent trans-Golgi localization and induction of membrane deformation." 京都大学 (Kyoto University), 2012. http://hdl.handle.net/2433/157901.
Повний текст джерелаDing, Jian. "Functional analysis of the extended N-terminus for the Drosophila Raf protein and initial characterization of the Arl1 gene." [Ames, Iowa : Iowa State University], 2010. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3403792.
Повний текст джерелаSharma, Prerna. "Unravelling the functional role of Arf-like GTPases 14 and 15 in mammalian cells." Thesis, 2022. https://etd.iisc.ac.in/handle/2005/5831.
Повний текст джерелаHsu, Hsin-Chia, and 許俽嘉. "Characterization of an Arl1p Guanine-Nucleotide Exchange Factor, Syt1p." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/04867349717273321965.
Повний текст джерела臺灣大學
分子醫學研究所
98
ARF-like (ARL) proteins belong to ADP-ribosylation factor (ARF) GTPase family, which are involved in protein trafficking and cytoskeleton organization. Those small G proteins require guanine-nucleotide exchange factors (GEFs) to switch from GDP-bound to GTP-bound form and become active. Previous reports suggested that Syt1p is the GEF of Arf2p and is involved in vesicle trafficking. Recently, our studies showed that Syt1p also acted as a GEF for Arl1p. In this study, Syt1p was further characterized. Firstly, it has been shown that Syt1p belongs to BFA-resistant GEFs. Secondly, Syt1p can use multiple regions to interact with Arl1p. The N-terminus, Sec7 domain, and C-terminus of Syt1p can all interact with Arl1d17N form, whose N-terminal first 17 amino acids are deleted. The interactions between all of the three regions and Arl1d17N are stronger than the interaction between full-length Syt1p and Arl1pd17N. Therefore, it might hint that Syt1p is autoregulated as other GEFs of Small GTPases. Surprisingly, we next found that Syt1p has an intramolecular interaction between the C-terminal region and Sec7 domain and an intermolecular interaction between C-terminal regions, indicating that Syt1p could form dimers or oligomers and might be autoregulated. Syt1p dimerization or oligomerization is also supported by in vivo pull down results, which proved that Syt1p can interact with itself. Moreover, the N-terminus is important for the formation of dimers or oligomers. Yeast two-hybrid screen was also performed to search for putative regulators of Syt1p. However, those candidates remain to be elucidated. Besides, whether dimerization or oligomerization plays an important role in Syt1p activation or membrane tethering and whether autoinhibition truly exists in Syt1p in vivo require further investigation.
LIn, Ching-Yi, and 林靜宜. "Functional Characterization of ADP-Ribosylation Factor-Like Proteins:ARL4 and ARL5." Thesis, 2001. http://ndltd.ncl.edu.tw/handle/37795439008511565193.
Повний текст джерела國立臺灣大學
分子醫學研究所
89
ADP-ribosylation factors (ARFs) Ras-related small GTP-binding proteins (~20 kDa), were originally identified as protein cofactors for the cholera toxin-catalyzed ADP-ribosylation of GS, the stimulatory subunit for adenylate cyclase. Their cofactor activity depends on GTP-binding- regulated by interactions with ARF-specific guanine nucleotide exchange factors (GEFs) or ARF-specific GTPase activating proteins (GAPs). Today, at least six mammalian ARF members have been identified and grouped into three classes. ARFs have been found in different subcellular localizations, and regulate several different vesicle transport steps in the exocytic and endocytic pathways- including budding from the endoplasmic reticulum and fusion to the Golgi stacks, endosomes, and nuclear vesicles. ARF-like (ARL) proteins, which belong to another subfamily of ARFs, have been cloned recently from Drosophila, rat, human and yeast. Although ARLs and ARFs have very similar amino acid sequences, ARLs lack cofactor activity for the cholera toxin-catalyzed ADP-ribosylation. dARL1 is essential in Drosophila, while disruption of yeast ARL1 gene is not lethal. ARL1 from yeast and human were reported to localize at the Golgi complex. In this thesis, we report the biochemical characterization and subcellular localizations of two ARLs- ARL4 and ARL5. We first cloned mouse and human ARL4 (mARL4 and hARL4) cDNA, respectively. Mice ARL4 is abundant in testis and has developmental stages-specific expression pattern. The appearance of mARL4 mRNA during embryonic development coincides with the sequential formation of somites and the establishment of brain compartmentation. Using ARL4-specific antibody in immuno-fluorescence microscopy, we found that endogenous mARL4 in cultured Sertoli and neuroblastoma cells was mainly concentrated in nuclei. When ectopically expressed in COS7 cells, ARL4-T34N mutant (predicted to be the GDP-bound form) was concentrated in nucleoli. Yeast two-hybrid screen and in vitro protein-interaction assays showed that hARL4 interacts with importin-a-required its C-terminal NLS region, and the interaction is nucleotide-independent. Like ARL2 and ARL3, recombinant hARL4 does not enhance cholera toxin-catalyzed auto-ADP-ribosylation. Its binding with GTPγS could be affected by phospholipid, and the N-terminus of hARL4, like that of ARF, is myristoylated. Our findings suggest that ARL4- with its distinctive nuclear/nucleolar localization and developmentally regulated expression pattern-may play a unique role(s) in neurogenesis and somitogenesis during embryonic development, and in the early stages of spermatogenesis in adults, respectively. Mouse and human ARL5 (mARL5 and hARL5) were also cloned, and the hARL5 mRNA is ubiquitously expressed in many tissues and considerably abundant in liver. mARL5 mRNA is mainly present at day 7 mouse embryos, then disappears at day 11. Our findings suggest that ARL5 may have an important role(s) in the early events of embryonic development. Immunostaining of COS7 cells transfected with Myc-tagged hARL5-WT, hARL5-T35N, hARL5-Q80L, and hARL5-dC constructs provide direct evidence for its subcellular localization in the cell. Interestingly, hARL5-T35N mutant, the predicted GDP-bound form, was most concentrated in nucleoli, but sometimes present in cytosol. By yeast two-hybrid screen, hARL5 interacts with NLS-receptor, importin-a, through the putative bipartite NLS in its C-terminal region. When NLS is removed from hARL5, hARL5-dC is colocalized with mitochondria; hARL5-T35N has the same pattern when it appears in the cytosol. In addition, yeast two-hybrid screen and in vitro protein-interaction assays showed that hARL5-WT, hARL5-Q80L can interact with HP1a, and the interaction is nucleotide-dependent. The interaction was further confirmed by in vivo protein-interaction assays. hARL5 contains MIR homology sequence- VPVLVL (residue 128~133)- that is crucial for hARL5 binding to HP1a. As ARL2, 3, and 4, recombinant hARL5 did not enhance the cholera toxin-catalyzed auto-ADP-ribosylation. Its intrinsic GTPgS-binding activity was low. The N-terminus of hARL5 is myristoylated as are ARFs. Based on these results, we have demonstrated that hARL5, like hARL4, with its specific interaction proteins and distinctive nuclear/nucleolar localizations may have important biological functions.
Diamantino, João Marques da Cunha dos Santos. "The role of Arl17 in healthy and influenza A virus infected cells." Master's thesis, 2019. http://hdl.handle.net/10362/89281.
Повний текст джерелаWu, Tsung-Shung. "Functional characterization of Arf-like protein, ARL5 and its interacting protein EB1." 2005. http://www.cetd.com.tw/ec/thesisdetail.aspx?etdun=U0001-0908200521130700.
Повний текст джерелаWu, Tsung-Shung, and 吳宗聖. "Functional characterization of Arf-like protein, ARL5 and its interacting protein EB1." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/81094559140885869980.
Повний текст джерела國立臺灣大學
分子醫學研究所
93
ADP-ribosylation factor like (ARL) proteins are one subfamily of ADP-ribosylation factor (ARF) small GTP binding protein family. Little is known about a human ARL protein, ARL5. Here we characterized the biologic properties and functions of hARL5 and described several novel observations. ARL5 expressed ubiquitously in many mammalian cell lines. In COS-7 cells, endogenous ARL5 and overexpressed GFP-ARL5 localized to centrosomes through out the cell cycle with exception of midbody localization during cytokinesis. By yeast two-hybrid screening, a microtubule plus-end binding protein EB1 was identified as an interacting partner of ARL5. ARL5 also interacted with EB1 in vivo. To investigate the biologic functions of ARL5, RNAi knockdown was performed. In ARL5 knockdown COS-7 cells, the microtubule regrowth from and anchoring at centrosomes were delayed and disordered similar to the defects caused by EB1 knockdown. Furthermore, overexpressed wild type and constitutively active form (ARL5Q80L) of ARL5 were diffused and partially localized to endosomes in COS-7 cells. The heterogeneous distributions of ARL5 constitutively inactive form (ARL5T35N) at endosomes, mitochondria, and aggresome-like compartments provided a distinct feature of ARL5. In addition, ARL5T35N diminished mitochondria membrane potential through its C-terminal region when it localized to mitochondria. Taken together, we infer that ARL5 might regulate different cellular processes, including centrosome-mediated microtubule nucleation and anchoring, vesicle trafficking, mitochondrial function, and protein degradation.
Kuo, Jer-Cheng, and 郭哲成. "Cloning and Characterization of Mammalian ADP-ribosylation Factor-like Proteins:ARL4 and ARL5." Thesis, 2000. http://ndltd.ncl.edu.tw/handle/91565491797612400017.
Повний текст джерела國立臺灣大學
分子醫學研究所
88
ADP-ribosylation factors(ARFs)are highly conserved ~20-kDa guanine nucleotide-binding proteins, which are believed to participate in vesicular trafficking in both endocytic and exocytic pathways. Several ARF-like proteins(ARLs)have been cloned, but their biological functions are still unknown. To characterize their molecular properties, we prepared ARL4- and ARL5-specific antibodies. In addition, human ARL4 mutants G2A, T34N, Q79L and deletion of C-terminus were respectively constructed. By library screening, we also cloned mouse ARL5 cDNA and genomic DNA. Our results indicated that mouse ARL5 mRNA was notably abundant in liver and heart. The appearance of mouse ARL5 mRNA during early embryonic development suggested that ARL5 might have played a fundamental role in embryogenesis. Using ARL4-specific antibody, we demonstrated that mouse ARL4 protein mainly presented in heart and colon. Furthermore, yeast two-hybrid screening showed that human ARL5 Q80L mutant, which was predicted to be in the GTP-bound state, interacted with α-catenin, heterochromatin protein 1α, N-methylpurine-DNA glycosylase and α-1-antichymotrypsin. Our findings proposed that ARL5 was possibly involved in nuclear functions. We provide some previous observation about mammalian ARL4 and ARL5 in this thesis.
Chen, Yan-Ting, and 陳彥廷. "Functional Characterization of small GTPase Arl1 and Golgin Protein Imh1 in Saccharomyces cerevisiae." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/5s8s72.
Повний текст джерела國立臺灣大學
分子醫學研究所
106
Arf-like proteins (Arls) are important regulators involved in a diversity of biological events, especially vesicle trafficking. In Saccharomyces cerevisiae, Arl1 acts to recruit a golgin protein Imh1 to the trans-Golgi network (TGN). However, besides the role of Imh1 as a high-copy suppressor of Ypt6, an important Rab protein mediating endosome-to-Golgi trafficking, less is known about it physiological significance. In previous studies (Hsu et al., 2016), they demonstrated that the Unfolded-Protein Response (UPR) augmented the activity of Arl1 and the subsequent Imh1 recruitment, but it remained to be elucidated on its specific functions under ER stress. Here, we showed that the UPR-activated Arl1 and Imh1 act to specifically maintain the endosome-to-Golgi trafficking when cell encounters ER stress. Moreover, this regulation does not simply depend on GARP complex recruitment, an important tethering complex, to affect retrograde trafficking. We found that the first five amino acids at Imh1 N-terminus is required for its function, as it contributes to the recruitment of Sft2, a tetra-spanning membrane protein involved in vesicle fusion. The N-terminus of Sft2 is responsible for facilitating the transport of Snc1 and Tlg1 and promoting retrograde trafficking. Together, our study is one of the first to demonstrate the physiological function of golgin Imh1 and elucidate the importance of the trafficking machinery in response to ER stress.
Huang, Hsiao-Chuan. "Functional characterization of human ADP-ribosylation factor like-1(ARL1) and its interacting proteins." 2006. http://www.cetd.com.tw/ec/thesisdetail.aspx?etdun=U0001-2807200600120100.
Повний текст джерелаHuang, Hsiao-Chuan, and 黃小娟. "Functional characterization of human ADP-ribosylation factor like-1(ARL1) and its interacting proteins." Thesis, 2006. http://ndltd.ncl.edu.tw/handle/77407680988503258813.
Повний текст джерела國立臺灣大學
分子醫學研究所
94
ADP-ribosylation factors (ARFs) and ARF-like proteins (ARLs) are members of the ARF family, which play essential roles in intracellular membrane trafficking. These proteins are regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) to cycle between active GTP-bound form and inactive GDP-bound form. ARLs are ~40–60 % identical to each other and to ARFs. Despite their high similarity to ARFs, only ARL1 has been shown to be involved in vesicular transport. ARL1 is localized in the Golgi complex and may participate in trans-Golgi network (TGN) to plasma membrane or endosome to TGN trafficking pathway. In the first part, we investigated the function of ARL1 by using constitutively active (Q71L) or inactive (T31N) ARL1. Discrepant with previous studies, we found that overexpressed ARL1Q71L specifically disperses Golgin-245 from Golgi apparatus. Over-expressed ARL1T31N disrupted trans-Golgi proteins but not cis/medial Golgi and endosome proteins. Moreover, VSVG transport was blocked in ARL1Q71L overexpressed but not in ARL1 knockdown cells which implied that ARL1 itself may not directly participate in the VSVG transport. In the second part, we attempted to find possible GAP for ARL1. Among our three candidates, ARFGAP1 did not interact with ARL1 in yeast two-hybrid assay but endogenous ARL1 were dissociated from the Golgi in cells with overexpressed ARFGAP1, which we considered an indirect consequence of general effect on Golgi proteins. Centaurin α1 neither interacted with ARL1 nor affected ARL1 localization. ARAP1 interacted with ARL1Q71LdN, but we could not detect the change of ARL1 localization when ARAP1 overexpressed. Whether ARAP1 could be GAP for ARL1 needs to be investigated further. In the third part, we identified an ARL1Q71L interacting protein, CIB1. We showed that ARL1 interacted with CIB1 in a Ca2+-dependent manner. Furthermore, CIB1 was ubiquitously expressed in cells especially colocalized with ARL1 in the Golgi apparatus in particular conditions. In addition, Golgi localization of CIB1 was not dependent on ARL1, and vice versa. Unfortunately, even though the interaction and colocalization of ARL1 and CIB1 were observed, we could not demonstrate the functional relevance between these two proteins.
Lasić, Maja [Verfasser]. "The yeast endosomal-, TGN-localized Ysl2p-Arl1p-Neo1p network : search for novel interaction partners / vorgelegt von Maja Lasić." 2008. http://d-nb.info/988929880/34.
Повний текст джерелаHuang, Lien Hung, and 黃連鴻. "Identification and characterization of arfaptin-1 as an effector and also a negative regulator of Arl1-mediated retrograde transport." Thesis, 2015. http://ndltd.ncl.edu.tw/handle/48369326865476347915.
Повний текст джерела長庚大學
生物醫學研究所
103
The small GTPase Arf-like protein 1 (Arl1) is well known for its role in intracellular vesicular transport at the trans-Golgi network (TGN). In here, we used differential affinity chromatography combined with mass spectrometry to identify Arf-interacting protein 1 (including arfaptin-1a and arfaptin-1b) as an Arl1-interacting protein. Yeast two-hybrid demonstrated that arfaptin-1 directly interacted with Arl1 through their arfaptin homolog (AH) domain. Arl1 knockdown caused arfaptin-1 dispersed from the Golgi apparatus. Expression of the wild-type Arl1, but not Arl1TN or wild-type Arf1 in Arl1- knockdown cells restored the Golgi localization of arfaptin-1. The Golgi dissociations of arfaptin-1 and Arl1 were temporally coupled in response to brefeldin-A treatment. These results demonstrated that Arl1 medicates the Golgi targeting of arfaptin-1. We also characterized a novel function for arfaptin-1 in Arl1-mediated retrograde transport. Using a Shiga-toxin subunit B (STxB) transportation assay, we demonstrated that knockdown of arfaptin-1 accelerated the retrograde transport of STxB from the endosome to the Golgi apparatus, whereas Arl1 knockdown inhibited STxB transport compared with control cells. Arfaptin-1 overexpression, but not an Arl1 binding-defective mutant (arfaptin-1b-F317A), consistently inhibited STxB transport. Exogenous arfaptin-1 expression did not interfere with the localization of the Arl1-interacting proteins golgin-97 and golgin-245 to the TGN and vice versa. Moreover, we found that the N-terminal region of arfaptin-1 was involved in the regulation of retrograde transport. Our results show that arfaptin-1 is an Arl1 effector and acts as a negative regulator in Arl1-mediated retrograde transport and suggest that different functional complexes containing Arl1 form in distinct microdomains and are responsible for different functions.
Barbosa, Sónia Cristina de Oliveira [Verfasser]. "Identification and characterization of Dop1p as an essential component of the Neo1p-Ysl2p-Arl1p membrane remodeling complex / vorgelegt von Sónia Cristina de Oliveira Barbosa." 2011. http://d-nb.info/1010950835/34.
Повний текст джерела