Gotowe bibliografie tematyczne / Arl14

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Gotowa bibliografia na temat „Arl14”

Autor: Grafiati
Data publikacji: 6 września 2023

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Artykuły w czasopismach na temat "Arl14"

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Brito, Cheila, Bruno Costa-Silva, Duarte C. Barral i Marta Pojo. "Unraveling the Relevance of ARL GTPases in Cutaneous Melanoma Prognosis through Integrated Bioinformatics Analysis". International Journal of Molecular Sciences 22, nr 17 (26.08.2021): 9260. http://dx.doi.org/10.3390/ijms22179260.

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Cutaneous melanoma (CM) is the deadliest skin cancer, whose molecular pathways underlying its malignancy remain unclear. Therefore, new information to guide evidence-based clinical decisions is required. Adenosine diphosphate (ADP)-ribosylation factor-like (ARL) proteins are membrane trafficking regulators whose biological relevance in CM is undetermined. Here, we investigated ARL expression and its impact on CM prognosis and immune microenvironment through integrated bioinformatics analysis. Our study found that all 22 ARLs are differentially expressed in CM. Specifically, ARL1 and ARL11 are upregulated and ARL15 is downregulated regardless of mutational frequency or copy number variations. According to TCGA data, ARL1 and ARL15 represent independent prognostic factors in CM as well as ARL11 based on GEPIA and OncoLnc. To investigate the mechanisms by which ARL1 and ARL11 increase patient survival while ARL15 reduces it, we evaluated their correlation with the immune microenvironment. CD4+ T cells and neutrophil infiltrates are significantly increased by ARL1 expression. Furthermore, ARL11 expression was correlated with 17 out of 21 immune infiltrates, including CD8+ T cells and M2 macrophages, described as having anti-tumoral activity. Likewise, ARL11 is interconnected with ZAP70, ADAM17, and P2RX7, which are implicated in immune cell activation. Collectively, this study provides the first evidence that ARL1, ARL11, and ARL15 may influence CM progression, prognosis, and immune microenvironment remodeling.
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Yang, Feng, Tiantian Li, Ziqing Peng, Yang Liu i Yusong Guo. "The amphipathic helices of Arfrp1 and Arl14 are sufficient to determine subcellular localizations". Journal of Biological Chemistry 295, nr 49 (24.09.2020): 16643–54. http://dx.doi.org/10.1074/jbc.ra120.014999.

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The subcellular localization of Arf family proteins is generally thought to be determined by their corresponding guanine nucleotide exchange factors. By promoting GTP binding, guanine nucleotide exchange factors induce conformational changes of Arf proteins exposing their N-terminal amphipathic helices, which then insert into the membranes to stabilize the membrane association process. Here, we found that the N-terminal amphipathic motifs of the Golgi-localized Arf family protein, Arfrp1, and the endosome- and plasma membrane–localized Arf family protein, Arl14, play critical roles in spatial determination. Exchanging the amphipathic helix motifs between these two Arf proteins causes the switch of their localizations. Moreover, the amphipathic helices of Arfrp1 and Arl14 are sufficient for cytosolic proteins to be localized into a specific cellular compartment. The spatial determination mediated by the Arfrp1 helix requires its binding partner Sys1. In addition, the residues that are required for the acetylation of the Arfrp1 helix and the myristoylation of the Arl14 helix are important for the specific subcellular localization. Interestingly, Arfrp1 and Arl14 are recruited to their specific cellular compartments independent of GTP binding. Our results demonstrate that the amphipathic motifs of Arfrp1 and Arl14 are sufficient for determining specific subcellular localizations in a GTP-independent manner, suggesting that the membrane association and activation of some Arf proteins are uncoupled.
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Zhang, Binbin, Aiqun Xu, Dong Wu, Wanli Xia, Pulin Li, Enze Wang, Rui Han, Peng Sun, Sijing Zhou i Ran Wang. "ARL14 as a Prognostic Biomarker in Non-Small Cell Lung Cancer". Journal of Inflammation Research Volume 14 (grudzień 2021): 6557–74. http://dx.doi.org/10.2147/jir.s340119.

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Yang, Yong-Kang, Hong Qu, Dong Gao, Wei Di, Hai-Wei Chen, Xin Guo, Zhong-He Zhai i Dan-Ying Chen. "ARF-like Protein 16 (ARL16) Inhibits RIG-I by Binding with Its C-terminal Domain in a GTP-dependent Manner". Journal of Biological Chemistry 286, nr 12 (13.01.2011): 10568–80. http://dx.doi.org/10.1074/jbc.m110.206896.

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Retinoic acid-inducible gene I (RIG-I) recognizes RNA virus-derived nucleic acids, which leads to the production of type I interferon (IFN) in most cell types. Tight regulation of RIG-I activity is important to prevent ultra-immune responses. In this study, we identified an ARF-like (ARL) family member, ARL16, as a protein that interacts with RIG-I. Overexpression of ARL16, but not its homologous proteins ARL1 and ARF1, inhibited RIG-I-mediated downstream signaling and antiviral activity. Knockdown of endogenous ARL16 by RNAi potentiated Sendai virus-induced IFN-β expression and vesicular stomatitis virus replication. ARL16 interacted with the C-terminal domain (CTD) of RIG-I to suppress the association between RIG-I and RNA. ARL16 (T37N) and ARL16Δ45–54, which were restricted to the GTP-disassociated form, did not interact with RIG-I and also lost the inhibitory function. Furthermore, we suggest that endogenous ARL16 changes to GTP binding status upon viral infection and binds with the RIG-I CTD to negatively control its signaling activity. These findings suggested a novel innate immune function for an ARL family member, and a GTP-dependent model in which RIG-I is regulated.
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Acosta-Herrera, Marialbert, Martin Kerick, David González-Serna, Cisca Wijmenga, Andre Franke, Peter K. Gregersen, Leonid Padyukov i in. "Genome-wide meta-analysis reveals shared new loci in systemic seropositive rheumatic diseases". Annals of the Rheumatic Diseases 78, nr 3 (20.12.2018): 311–19. http://dx.doi.org/10.1136/annrheumdis-2018-214127.

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ObjectiveImmune-mediated inflammatory diseases (IMIDs) are heterogeneous and complex conditions with overlapping clinical symptoms and elevated familial aggregation, which suggests the existence of a shared genetic component. In order to identify this genetic background in a systematic fashion, we performed the first cross-disease genome-wide meta-analysis in systemic seropositive rheumatic diseases, namely, systemic sclerosis, systemic lupus erythematosus, rheumatoid arthritis and idiopathic inflammatory myopathies.MethodsWe meta-analysed ~6.5 million single nucleotide polymorphisms in 11 678 cases and 19 704 non-affected controls of European descent populations. The functional roles of the associated variants were interrogated using publicly available databases.ResultsOur analysis revealed five shared genome-wide significant independent loci that had not been previously associated with these diseases: NAB1, KPNA4-ARL14, DGQK, LIMK1 and PRR12. All of these loci are related with immune processes such as interferon and epidermal growth factor signalling, response to methotrexate, cytoskeleton dynamics and coagulation cascade. Remarkably, several of the associated loci are known key players in autoimmunity, which supports the validity of our results. All the associated variants showed significant functional enrichment in DNase hypersensitivity sites, chromatin states and histone marks in relevant immune cells, including shared expression quantitative trait loci. Additionally, our results were significantly enriched in drugs that are being tested for the treatment of the diseases under study.ConclusionsWe have identified shared new risk loci with functional value across diseases and pinpoint new potential candidate loci that could be further investigated. Our results highlight the potential of drug repositioning among related systemic seropositive rheumatic IMIDs.
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Wicky, Sidonie, Heinz Schwarz i Birgit Singer-Krüger. "Molecular Interactions of Yeast Neo1p, an Essential Member of the Drs2 Family of Aminophospholipid Translocases, and Its Role in Membrane Trafficking within the Endomembrane System". Molecular and Cellular Biology 24, nr 17 (1.09.2004): 7402–18. http://dx.doi.org/10.1128/mcb.24.17.7402-7418.2004.

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ABSTRACT Neo1p is an essential yeast member of the highly conserved Drs2 family of P-type ATPases with proposed aminophospholipid translocase activity. Here we present evidence that Neo1p localizes to endosomes and Golgi elements. In agreement with that finding, the temperature-sensitive neo1-37 and neo1-69 mutants exhibit defects in receptor-mediated endocytosis, vacuole biogenesis, and vacuolar protein sorting. Furthermore, neo1 mutants accumulate aberrantly shaped membranous structures most likely derived from vacuoles and the endosomal/Golgi system. At permissive temperatures, HA-Neo1-69p, like wild-type Neo1p, is stable and associates with endosomes. In contrast, HA-Neo1-37p is rapidly degraded and is predominantly retained within the endoplasmic reticulum (ER). Thus, the two neo1 alleles affect the stability and localization of the mutant polypeptides in different ways. A C-terminally truncated and a C-terminally epitope-tagged version of Neo1p are nonfunctional and also mislocalize to the ER. In agreement with a role within the endomembrane system, Neo1p exhibits genetic and physical interactions with Ysl2p, a potential guanine nucleotide exchange factor for Arl1p. Interestingly, deletion of ARL1 rescues the temperature sensitivity of neo1-37 and neo1-69. We demonstrate that Arl1p in its myristoylated and GTP-bound form is responsible for the inhibitory effect. Thus, Neo1p, Ysl2p, and Arl1p represent three proteins that collaborate in membrane trafficking within the endosomal/Golgi system.
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Zolotarov, Yevgen, Chao Ma, Irene González-Recio, Serge Hardy, Gijs A. C. Franken, Noriko Uetani, Femke Latta i in. "ARL15 modulates magnesium homeostasis through N-glycosylation of CNNMs". Cellular and Molecular Life Sciences 78, nr 13 (5.06.2021): 5427–45. http://dx.doi.org/10.1007/s00018-021-03832-8.

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AbstractCyclin M (CNNM1-4) proteins maintain cellular and body magnesium (Mg2+) homeostasis. Using various biochemical approaches, we have identified members of the CNNM family as direct interacting partners of ADP-ribosylation factor-like GTPase 15 (ARL15), a small GTP-binding protein. ARL15 interacts with CNNMs at their carboxyl-terminal conserved cystathionine-β-synthase (CBS) domains. In silico modeling of the interaction between CNNM2 and ARL15 supports that the small GTPase specifically binds the CBS1 and CNBH domains. Immunocytochemical experiments demonstrate that CNNM2 and ARL15 co-localize in the kidney, with both proteins showing subcellular localization in the endoplasmic reticulum, Golgi apparatus and the plasma membrane. Most importantly, we found that ARL15 is required for forming complex N-glycosylation of CNNMs. Overexpression of ARL15 promotes complex N-glycosylation of CNNM3. Mg2+ uptake experiments with a stable isotope demonstrate that there is a significant increase of 25Mg2+ uptake upon knockdown of ARL15 in multiple kidney cancer cell lines. Altogether, our results establish ARL15 as a novel negative regulator of Mg2+ transport by promoting the complex N-glycosylation of CNNMs.
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Hsu, Jia-Wei, Pei-Hua Tang, I.-Hao Wang, Chia-Lun Liu, Wen-Hui Chen, Pei-Chin Tsai, Kuan-Yu Chen, Kuan-Jung Chen, Chia-Jung Yu i Fang-Jen S. Lee. "Unfolded protein response regulates yeast small GTPase Arl1p activation at late Golgi via phosphorylation of Arf GEF Syt1p". Proceedings of the National Academy of Sciences 113, nr 12 (10.03.2016): E1683—E1690. http://dx.doi.org/10.1073/pnas.1518260113.

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ADP ribosylation factor (Arf) GTPases are key regulators of membrane traffic at the Golgi complex. In yeast, Arf guanine nucleotide-exchange factor (GEF) Syt1p activates Arf-like protein Arl1p, which was accompanied by accumulation of golgin Imh1p at late Golgi, but whether and how this function of Syt1p is regulated remains unclear. Here, we report that the inositol-requiring kinase 1 (Ire1p)-mediated unfolded protein response (UPR) modulated Arl1p activation at late Golgi. Arl1p activation was dependent on both kinase and endo-RNase activities of Ire1p. Moreover, constitutively active transcription factor Hac1p restored the Golgi localization of Arl1p and Imh1p inIRE1-deleted cells. Elucidating the mechanism of Ire1p–Hac1p axis actions, we found that it regulated phosphorylation of Syt1p, which enhances Arl1p activation, recruitment of Imh1p to the Golgi, and Syt1p interaction with Arl1p. Consistent with these findings, the induction of UPR by tunicamycin treatment increases phosphorylation of Syt1p, resulting in Arl1p activation. Thus, these findings clarify how the UPR influences the roles of Syt1p, Arl1p, and Imh1p in Golgi transport.
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Liu, Ya-Wen, Chun-Fang Huang, Kai-Bin Huang i Fang-Jen S. Lee. "Role for Gcs1p in Regulation of Arl1p atTrans-Golgi Compartments". Molecular Biology of the Cell 16, nr 9 (wrzesień 2005): 4024–33. http://dx.doi.org/10.1091/mbc.e05-01-0023.

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ADP-ribosylation factor (ARF) and ARF-like (ARL) proteins are members of the ARF family, which are critical components of several different vesicular trafficking pathways. ARFs have little or no detectable GTPase activity without the assistance of a GTPase-activating protein (GAP). Here, we demonstrate that yeast Gcs1p exhibits GAP activity toward Arl1p and Arf1p in vitro, and Arl1p can interact with Gcs1p in a GTP-dependent manner. Arl1p was observed both on trans-Golgi and in cytosol and was recruited from cytosol to membranes in a GTP-dependent manner. In gcs1 mutant cells, the fraction of Arl1p in cytosol relative to trans-Golgi was less than it was in wild-type cells. Increasing Gcs1p levels returned the distribution toward that of wild-type cells. Both Arl1p and Gcs1p influenced the distribution of Imh1p, an Arl1p effector. Our data are consistent with the conclusion that Arl1p moves in a dynamic equilibrium between trans-Golgi and cytosol, and the release of Arl1p from membranes in cells requires the hydrolysis of bound GTP, which is accelerated by Gcs1p.
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Xie, Ning, Qiuai Shu, Ziwei Wang, Xindi Huang, Yalan Wang, Bin Qin, Yan Chen i in. "ARL11 correlates with the immunosuppression and poor prognosis in breast cancer: A comprehensive bioinformatics analysis of ARL family members". PLOS ONE 17, nr 11 (11.11.2022): e0274757. http://dx.doi.org/10.1371/journal.pone.0274757.

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ADP-ribosylation factor-like protein (ARL) family members (ARLs) may regulate the malignant phenotypes of cancer cells. However, relevant studies on ARLs in breast cancer (BC) are limited. In this research, the expression profiles, genetic variations, and prognostic values of ARLs in BC have been systematically analyzed for the first time using various databases. We find that ARLs are significantly dysregulated in BC according to the TCGA database, which may result from DNA methylation and copy number alteration. Prognostic analysis suggests that ARL11 is the most significant prognostic indicator for BC, and higher ARL11 predicts worse clinical outcomes for BC patients. Further functional enrichment analysis demonstrates that ARL11 enhances the immunosuppression in BC, and dysregulation of ARL11 is significantly associated with immune infiltration in various types of cancer. Our results demonstrate the potential of ARL11 as an immune therapeutic target for BC.
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Rozprawy doktorskie na temat "Arl14"

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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.

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Hofmann, Irmgard Maria Rita. "Characterisation of the human Arl4 and Arl8 families of small GTPases". Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.604140.

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Two closely related human Arls, Arl8a and Arl8b, were found to localise to lysosomes in mammalian cells. conventionally, membrane binding of Arf and Arl proteins is mediated by both an N-terminal myristoyl group and an N-terminal amphipathic helix that are inserted into the lipid bilayer upon activation of the GTPase. Arl8 GPTases lack myristolylation sites, and examination of the N-terminus of Arl8b revealed that it contains an acetyl group instead, and this acetylated methionine is necessary for its lysosomal location. Lysosomes of cells overexpressing Arl8b move more frequently, suggesting a role for Arl8a and Arl8b as positive regulators of lysosomal transport. Arl4a, Arl4c and Arl4d are very similar in sequence and were found to act in a pathway upstream of Arf6, Arf6 is a regulator of key processes at the plasma membrane, such as endocytosis, actin dynamics and cell adhesion. One of the major activators of Arf6 is the exchange factor ARNO (‘Arf nucleotide binding site opener’). In order to activate Arf6, ARNO must translocate from the cytoplasm onto the plasma membrane. ARNO was identified as an interaction partner of Arl4 GTPases in a yeast two hybrid screen, and Arl4 GTPases mediate membrane translocation of ARNO. Thus, Arl4 GTPases represent a novel signal transduction pathway upstream of Arf6. This study provides a characterisation of members of the human Arl family and suggests functions for Arl4 and Arl8 GTPases in membrane traffic related processes.
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Lasić, 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.

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Man, 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.

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Ding, 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.

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Man, Hon-wai, i 文漢威. "A study of zebrafish hematopoiesis based on chemical screening and gene knock-down by morpholino with particular reference to ADP-ribosylation factor like 4 (ARL4)". Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2011. http://hub.hku.hk/bib/B47770521.

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Zebrafish has emerged as an important vertebrate model for studying hematopoiesis and its genetic and chemical modifiers. The zebrafish embryos are unique in their optical transparency, ease of maintenance and high fecundity. They are also amendable to genetic and pharmacological perturbation at high throughput. As a result, the embryos are suitable for various experimental techniques and have a high efficiency in large-scale drug screening. Recently, zebrafish has also emerged as a model for the study of human disease. In this model organism, primitive hematopoiesis is transitory and it occurs in the intermediate cells mass and comprises primarily erythroid cells. Definitive hematopoiesis arises from the ventral wall of dorsal aorta and moves to the caudal hematopoietic tissues, thence the kidney, where life-long and multi-lineage differentiation occurs. The chemical screening platform comprises O-dianisidine staining for hemoglobin containing cells (erythroid) during primitive hematopoiesis. Positive hits were validated based on flow cytometry of dissociated transgenic Tg(gata1:GFP) embryos and whole-mount in-situ hybridization (WISH) for hematopoietic genes. Gene knock-down was conducted by morpholinos (MO) injected into zebrafish embryos at 1-4 cell stage and the effects on hematopoietic development evaluated by WISH and quantitative real-time PCR. Chemical screening of 74 compounds has been performed. These compounds were obtained from a chemical library comprising 879 compounds from NIH (National Institutes of Health) and pre-screened by their effects on cancer cell lines. Four compounds (Tin(IV), chlorotriphenyl [1-(4-ethoxyphenyl)- 3-cyanoureato]-hydrogen,triethylamine, Nogamycin, N,N-Dibenzyldaunorubicin hydrochloride and Allyl 2,3,4-tri-O-benzyl-6-O-(tert-butyldimethylsilyl)-α- D-gluco-Pyranoside) which significantly reduced O-dianisidine staining were identified of which one (Allyl 2,3,4-tri-O-benzyl-6-O-(tert-butyldimethylsilyl) -α-D-glucopyranoside was shown to reduce GFP+ population in Tg(gata1:GFP) population Another chemical (2-Propanol,1,1'-[(1-methylethylidene)bis(4, 1-phenyleneoxy)]bis[3-[(1,1,3,3-tetramethylbutyl)amino]-,dihydrochloride]) was shown to reduce c-myb (marker of definitive hematopoiesis) expression in the ventral wall of dorsal aorta. I also attempted gene knock in zebrafish embryos based on anti-sense morpholino microinjection. A gene encoding for arl4ab was examined, as it was shown to be expressed in hematopoietic tissue in zebrafish embryos but its function is entirely unknown. Knock-down of arl4ab significantly reduced c-myb and runx1 expression in the ventral wall of dorsal aorta and it can be reversed by co-injecting arl4ab mRNA. scl and gata1 expression as well as GFP expression in transgenic Tg(flk1:GFP) embryos that represented vascular development was unaffected. In summary, a zebrafish platform for the study of chemical and genetic modifiers was established. The results have provided important leads for further study into the mechanisms whereby these modifiers regulate hematopoiesis in the zebrafish embryos.
published_or_final_version
Medicine
Master
Master of Medical Sciences
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Hsu, Hsin-Chia, i 許俽嘉. "Characterization of an Arl1p Guanine-Nucleotide Exchange Factor, Syt1p". Thesis, 2010. http://ndltd.ncl.edu.tw/handle/04867349717273321965.

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碩士
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.
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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.

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Influenza A virus (IAV) is an important human pathogen that causes epidemic and pandemic events of flu. The study of the viral life cycle and its interactions with the infected host is crucial for the development of novel therapeutic strategies. IAV has an eight-part segmented RNA genome organized in viral ribonucleoprotein complexes (vRNP), which are replicated in the nucleus of the cell. De novo synthesized vRNPs need to leave the nucleus to reach the cytosol for viral assembly, budding and release. Several pathways have been implicated in nuclear export of vRNPs, including CRM1, apoptosis activation and extracellular signal-regulated kinase 1 and 2 (ERK1/2) signaling cascade. Mitochondria are crucial organelles for the maintenance of cellular homeostasis, since they are responsible for the regulation of metabolism, apoptosis, calcium homeostasis and innate immunity. Their functions are tightly regulated by dynamic changes in mitochondrial morphology. Given their importance, many viruses modulate mitochondria to promote cellular environments favoring their proliferation. IAV has been shown to fragment mitochondria to decrease the antiviral immune response. Our lab identified a candidate modulator of mitochondrial morphology and IAV infection: the host GTPase Arl17. Our work demonstrated that depletion of Arl17 leads to a reduction in viral titers and promotes mitochondrial fragmentation, regardless of infection. Interestingly, this phenotype was not accompanied by alterations in IFNβ1 expression and mitochondrial unfolded protein response activation (UPRmt). However, ATP levels were significantly reduced in the absence of Arl17. Additionally, we showed that Arl17 is required for regular vRNP nuclear export. In its absence, we observed a delay in vRNPs nuclear export that was CRM1- and ERK1/2-independent. Therefore, influence of Arl17 on the induction of apoptosis should be further investigated as its inhibition could explain vRNPs nuclear export delay and it could be the element that links mitochondria and vRNPs nuclear export.
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Chen, Yan-Ting, i 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.

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碩士
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.
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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.

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Książki na temat "Arl14"

1

Tanning & Dressing of Leather (UK Markets: Annual Reports 1994: AR14). The Stationery Office Books (Agencies), 1996.

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Tanning & Dressing of Leather (UK Markets: Annual Reports 1993: AR14). The Stationery Office Books (Agencies), 1994.

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Części książek na temat "Arl14"

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Merchel, Joachim. "Hilfeplanung". W Handbuch Allgemeiner Sozialer Dienst (ASD), 3. aktual. u. erw. Auflage. München: Ernst Reinhardt Verlag, 2019. http://dx.doi.org/10.2378/asda3.art14.

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Konu, Ari, i Eero Pekkarinen. "Université provinciale de Laponie". W Politiques et gestion de l'enseignement supérieur, Volume 20 Numéro 2, 1–11. OECD, 2008. http://dx.doi.org/10.1787/hemp-v20-art14-fr.

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Pacheco-Rodriguez, Gustavo, Joel Moss i Martha Vaughan. "[44] Preparation and assay of recombinant ADP-ribosylation factor-like protein-1 (ARL1)". W Methods in Enzymology, 424–28. Elsevier, 2001. http://dx.doi.org/10.1016/s0076-6879(01)29103-4.

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Tai, Guihua, Lei Lu, Ludger Johannes i Wanjin Hong. "Functional Analysis of Arl1 and Golgin‐97 in Endosome‐to‐TGN Transport Using Recombinant Shiga Toxin B Fragment". W Methods in Enzymology, 442–53. Elsevier, 2005. http://dx.doi.org/10.1016/s0076-6879(05)04039-5.

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Lu, Lei, Guihua Tai i Wanjin Hong. "Interaction of Arl1 GTPase with the GRIP Domain of Golgin‐245 as Assessed by GST (Glutathione‐S‐transferase) Pull‐Down Experiments". W Methods in Enzymology, 432–41. Elsevier, 2005. http://dx.doi.org/10.1016/s0076-6879(05)04038-3.

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Streszczenia konferencji na temat "Arl14"

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Mueller, Eduarda, Julia Volkmann, Jonathan Utzig i Henry França Meier. "ANÁLISE DOS FORMATOS GEOMÉTRICOS DE ANÉIS DEFLETORES INTERNOS EM ESCOAMENTO GÁS-SÓLIDO EM RISERS". W Simpósio Paranaense de Modelagem, Simulação e Controle de Processos. Departamento de Engenharia Química UFPR, 2020. http://dx.doi.org/10.5380/simproc4.2019.art14.

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Ramirez, Mariano. "DESIGN FOR OTHER SPECIES: AUSTRALIAN EXAMPLES". W Simpósio de Design Sustentável. Departamento de Design da UFPR, 2021. http://dx.doi.org/10.5380/8sds2021.art14.

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Lee, Sooyong, Sangkyou Lee, Jolanta Bondaruk, Hua Wang, Shizhen Zhang, Menashe Bar-Eli, Peter Black i in. "Abstract 3065: Loss of ARL11 function promotes growth ofin situneoplasia by activating the ras pathway". W Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3065.

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"СЕМЕЙНЫЕ АРХИВЫ. «БОЛЬШАЯ» ИСТОРИЯ В ЧАСТНОМ ПРЕЛОМЛЕНИИ". W НА ПЕРЕКРЕСТКЕ СЕВЕРА И ВОСТОКА (МЕТОДОЛОГИИ И ПРАКТИКИ РЕГИОНАЛЬНОГО РАЗВИТИЯ). Science and Innovation Center Publishing House, 2023. http://dx.doi.org/10.12731/978-5-907608-10-8-art14.

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Raporty organizacyjne na temat "Arl14"

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Divan, Brooke, Richard Lampo i Lawrence Clark. Demonstration of a standard steel coating system modified with a vapor-phase corrosion inhibitor : final report on Project F12-AR14. Engineer Research and Development Center (U.S.), wrzesień 2018. http://dx.doi.org/10.21079/11681/29516.

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