Добірка наукової літератури з теми "Beta arrestin signaling"
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Статті в журналах з теми "Beta arrestin signaling"
Nogueras-Ortiz, Carlos, Cristina Roman-Vendrell, Gabriel E. Mateo-Semidey, Yu-Hsien Liao, Debra A. Kendall, and Guillermo A. Yudowski. "Retromer stops beta-arrestin 1–mediated signaling from internalized cannabinoid 2 receptors." Molecular Biology of the Cell 28, no. 24 (November 15, 2017): 3554–61. http://dx.doi.org/10.1091/mbc.e17-03-0198.
Повний текст джерелаPatel, Priyesh A., Douglas G. Tilley, and Howard A. Rockman. "Beta-Arrestin-Mediated Signaling in the Heart." Circulation Journal 72, no. 11 (2008): 1725–29. http://dx.doi.org/10.1253/circj.cj-08-0734.
Повний текст джерелаMa, L., and G. Pei. "beta-arrestin signaling and regulation of transcription." Journal of Cell Science 120, no. 2 (January 15, 2007): 213–18. http://dx.doi.org/10.1242/jcs.03338.
Повний текст джерелаLaporte, S. A., and M. G. Caron. "Beta-arrestin and GPCR desensitization, internalization, and signaling." Biochemical Society Transactions 29, no. 3 (June 1, 2001): A64. http://dx.doi.org/10.1042/bst029a064.
Повний текст джерелаLee, Claudia, Gayathri Viswanathan, Issac Choi, Chanpreet Jassal, Taylor Kohlmann, and Sudarshan Rajagopal. "Beta-Arrestins and Receptor Signaling in the Vascular Endothelium." Biomolecules 11, no. 1 (December 23, 2020): 9. http://dx.doi.org/10.3390/biom11010009.
Повний текст джерелаConley, Jason M., and Hongxia Ren. "Human GPR17 Nonsynonymous Variants Identified in Individuals with Metabolic Diseases Have Distinct Functional Signaling Profiles." Journal of the Endocrine Society 5, Supplement_1 (May 1, 2021): A656. http://dx.doi.org/10.1210/jendso/bvab048.1337.
Повний текст джерелаCarneiro de Morais, Carla P., Juliano Z. Polidoro, Donna L. Ralph, Thaissa D. Pessoa, Maria Oliveira-Souza, Valério G. Barauna, Nancy A. Rebouças, Gerhard Malnic, Alicia A. McDonough, and Adriana C. C. Girardi. "Proximal tubule NHE3 activity is inhibited by beta-arrestin-biased angiotensin II type 1 receptor signaling." American Journal of Physiology-Cell Physiology 309, no. 8 (October 15, 2015): C541—C550. http://dx.doi.org/10.1152/ajpcell.00072.2015.
Повний текст джерелаWisler, J. W., S. M. DeWire, E. J. Whalen, J. D. Violin, M. T. Drake, S. Ahn, S. K. Shenoy, and R. J. Lefkowitz. "A unique mechanism of beta-blocker action: Carvedilol stimulates beta-arrestin signaling." Proceedings of the National Academy of Sciences 104, no. 42 (October 9, 2007): 16657–62. http://dx.doi.org/10.1073/pnas.0707936104.
Повний текст джерелаHurst, Dow P., Diane L. Lynch, Derek M. Shore, Michael C. Pitman, and Patricia H. Reggio. "Beta-Arrestin Biased Signaling at a Class a GPCR: Modeling the ORG27569 Induced CB1/Beta-Arrestin 1 Complex." Biophysical Journal 108, no. 2 (January 2015): 97a. http://dx.doi.org/10.1016/j.bpj.2014.11.557.
Повний текст джерелаYin, Deling, Hui Yan, Hui Li, Christopher Daniels, Krishna Singh, Balvin Chua, Charles Stuart, Yi Caudle, and Gene LeSage. "Beta-arrestin 2 plays a critical role in sepsis-induced cardiac dysfunction." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 124.4. http://dx.doi.org/10.4049/jimmunol.196.supp.124.4.
Повний текст джерелаДисертації з теми "Beta arrestin signaling"
Sharmeen, Cynthia. "Involvement of Beta-arrestin 1 and Beta-arrestin 2 in store operated calcium entry." Mémoire, Université de Sherbrooke, 2016. http://hdl.handle.net/11143/9499.
Повний текст джерелаAbstract : In an organism, intracellular [Ca2+] takes part in many biological processes. Eukaryotic cells express a variety of channels in the plasma membrane through which calcium can enter. In non-excitable cells, two main mechanisms allow calcium entry; the store-operated calcium entry via Orai1 (SOCE) and receptor-operated calcium entry (ROCE). Several key proteins are involved in the regulation of these calcium entry pathways as well as in calcium homeostasis. TRPC6 is a calcium channel implied in calcium entrance into the cells following hormonal stimulation and translocates to the plasma membrane. TRPC6 channel appear to the plasma membrane until the stimulus is present. Although, the mechanisms that regulate the trafficking and activation of TRPC6 are still little known. Recent findings have demonstrated that there is a potential role of Rho kinase in activity of TRPC6. Rho kinase is activated by the small G protein RhoA that itself can be activated by the heterotrimeric G proteins Gα12 and Gα13. In addition to Gα12 and Gα13 proteins, cytosolic GPCR desensitizing proteins β-arrestin 1 and/or β-arrestin 2 could also activate RhoA. The purpose of our study is to investigate the involvement of the proteins Gα12/13 and β-arrestin 1/β-arrestin 2 in the activation of TRPC6 and Orai1 protein. We used siRNA specific to Gα12/13 or β-arrestin 1/β-arrestin 2 to knockdown their endogenous expression. Then, calcium imaging in real time was performed in order to see the quantity of calcium entered into the cell following stimulation by vasopressin (AVP), thapsigargin, or carbachol. We hence identified that in A7r5 cell, vascular smooth muscle cell where TRPC6 channel expressed endogenously; reduced expression of Gα12 or Gα13 proteins does not seem to modify the AVP-induced Ca2+ entry compared to control cells. On the other hand, calcium imaging experiment in knocked down β-arrestin 1 or β-arrestin 2 in HEK 293 cells as well as HEK 293 cells stably transfected with TRPC6 (T6.11 cells) resulted in an increased thapsigargin-induced calcium entry. The co-immunoprecipitation studies demonstrate an interaction between β-arrestin 1 and STIM1, a calcium sensor in SOCE influx, while no interaction was observed between β-arrestin 1 and Orai1.We moreover showed by confocal microscopy that reduced expression of β-arrestin 1/ β-arrestin 2 does not influence the quantity of Orai1 at the cell periphery. Preliminary results showed that reduced expression of β-arrestin 1 or β-arrestin 2 increases the quantity of STIM1-YFP in the intracellular space and less it’s in peri-membrane space. In conclusion, we showed that β-arrestin 1 or β-arrestin 2 are involved in the store-operated calcium entry (SOCE) and control the quantity of STIM1 in the endoplasmic reticulum.
Witty, Marie-France. "Role of the adaptor protein, beta-arrestin1, in the Notch signaling pathway." Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/446.
Повний текст джерелаZimmerman, Brandon. "Regulation of angiotension II type I receptor signalling by beta-arrestin and the clathrin adaptor AP-2." Thesis, McGill University, 2012. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=107645.
Повний текст джерелаLes récepteurs couplés aux protéines G (RCPGs) jouent un rôle fondamental dans notre équilibre homéostatique par leur implication dans de nombreux processus physiologiques. Afin de maintenir leur réactivité à l'environnement extracellulaire, un processus complexe de désensibilisation et resensibilisation des récepteurs a évolué. Afin de permettre aux récepteurs d'être resensibilisés, ils doivent d'abord être internalisés par endocytose, un processus impliquant de nombreuses protéines adaptatrices. La méthode la plus commune de l'internalisation des RCPGs est la voie dépendante à la clathrine, où les deux adaptateurs les plus importants sont βarrestine et AP-2. Bien que nous ayons une image relativement claire de la façon dont ces protéines conduisent à l'endocytose du récepteur, les mécanismes de régulation où ces adaptateurs de l'endocytose peuvent affecter ou être affecté par des processus de signalisation sont nettement moins bien décrits. Le récepteur de l'angiotensine II de type I est utilisé comme récepteur modèle dans nos études. Les études antérieures de notre laboratoire ont caractérisé certains des facteurs protéiques nécessaires pour le processus d'endocytose. Bien que les études précédentes ont démontré une régulation dépendante à la phosphorylation des complexes βarrestine et AP-2, ces résultats ont été exclusivement in vitro et n'ont pas été confirmés dans les cellules vivantes. Nous avons généré un anticorps polyclonal dirigé contre le site de phosphorylation putatif et avons révélé que non seulement cet évènement de phosphorylation se produit dans plusieurs types de cellules en réponse au traitement à l'angiotensine II (AngII), mais que l'activation de récepteurs multiples, comprenant un non-RCPG, le récepteur du facteur de croissance de l'épiderme, induisait la phosphorylation sur l'unité β de AP-2. Mon travail, précédemment publié dans un manuscrit, a également révélé que la prévention de cet évènement de phosphorylation stabilise les complexes βarrestine/AP-2 de façon significative. Bien que nos études initiales aient révélé que cette phosphorylation a peu d'impact sur l'endocytose des récepteurs, de nouveaux outils ont depuis été développés dans le laboratoire. Premièrement, nous avons généré un anticorps à chaîne unique qui peut être exprimé de façon intracellulaire et cible les phosphosites, et avons démontré que la liaison à ce résidu phosphorylé résulte dans un arrêt prolongé de l'endocytose. Nous avons également démontré que ce résidu tyrosine phosphorylé est un motif putatif de liaison pour certaines protéines contenant un domaine SH2 étant donné que trois de ces protéines sont capables de se lier à une β2adaptine phosphorylée. Enfin, en raison de la nature dépendate à βarrestine de cet évènement de phosphorylation, nous avons characterise quatre analogies de AngII avec une seule substitution d'acide amine dans leur sequence octapeptidique. Nos conclusions établissent une relation corrélative entre la force d'avidité de βarrestine pour son récepteur et le niveau d'activation de la kinase ERK suite aux signaux extracellulaires. Vraisemblablement, les différences d'avidité modifient le trafic du récepteur dans son destin vers le recyclage ou la dégradation. Par ailleurs, nous établissons que la conformation de βarrestine peut altérer les voies activées en aval du récepteur, entraînant d'autres effets cellulaires comme la croissance cellulaire ou la migration. Ces résultats mettent en évidence l'importance de la régulation par ces adaptateurs de l'endocytose sur le destin du RCPG, non seulement par leur rôle dans l'internalisation, mais aussi par leur propre potentiel de signalisation.
De, pascali Francesco. "Allosteric modulation of follicle stimulating hormone receptor and GPR54 : new tools to study signalling." Thesis, Tours, 2019. http://www.theses.fr/2019TOUR4030.
Повний текст джерелаGPR54 and FSHR regulate reproduction by acting on the hypothalamus-pituitary-gonads (HPG) axis. Acting in the hypothalamus, GPR54 is an upstream regulator of the axis whereas FSHR controls gametogenesis in both sexes. They represents two major pharmacological targets for the treatment of fertility-related problems. Both GPR54 and FSHR belong to the G protein-coupled receptor (GPCR) superfamilly. GPR54 preferentially activates the Gαq/PLC/Ca2+ pathway whereas FSHR mainly activates the Gαs/PKA/cAMP pathway. Both receptors recruit and activate β-arrestins. Increasing number pharmacological profiles have been reported to act on GPCR. Indeed biased ligands capable of preferentially eliciting a subset of the full signalling repertoire, compared to the endogenous ligand are discovered at a high rate. Orthosteric and allosteric ligands can both induce biased signalling by stabilizing specific receptor conformations. Therapeutically, biased ligand have demonstrated the potential to avoid side effects while still activating the signalling pathways leading to therapeutic effects. Moreover, allosteric ligands allow positive or negative modulation of a receptor while keeping the temporal information provided by the endogenous ligand. Until recently, such diverse and valuable pharmacological tools were not available for FSHR and GPR54. The aim of this thesis was to identify allosteric ligands at the FSHR and GPR54 and to characterize their biased signalling. In the first section, we pharmacological characterized a panel of low molecular weight ligands, recently reported to allosterically activate the FSHR and belonging to two chemical classes. We profiled their actions on different signalling pathways in living HEK293 cells expressing different biosensors. We demonstrated each of these compounds induced biased signalling at the FSHR compared to FSH. Using different cell models, we confirmed that system bias is a crucial confounding factor in bias determination. We also identified limit cases in which the operational model did not allow to calculated bias factors. In parallel, we characterized two novel compounds belonging to chemical classes that were not yet reported to activate FSHR. We demonstrated that they were allosteric and that their biased profiles were distinct from the compounds characterized in the first study. In second section of the thesis, we selected and pharmacological characterized nanobodies targeting GPR54 and FSHR. We identified a nanobody that behaved as a positive allosteric modulator (PAM) at the GPR54. We also identified a nanobody against FSHR. This nanobody displayed striking biased properties as it was negative allosteric modulator (NAM) for cAMP production but PAM for β-arrestin 2 recruitment. In the last section of the thesis, we attempted to develop nanobody-drug conjugates (NDC) by linking our nanobodies to agonists - either kisspeptin or one of the low molecular weight agonist of the FSHR - through a flexible linker. Though we did not have time to achieve a proof of concept for NDC, we believe that such hybrid compound could represent at minimum a promising research tools. As a whole, this thesis provides novel pharmacological tools that should allow deciphering the relative contributions of the different transduction mechanisms operating at the FSHR and GPR54, in vivo, in the reproductive function. This work also opens possible avenues for future therapeutic strategies in the control of reproduction in farm animals and in reproductive medicine
Davenport, Chandra. "Hedgehog Signaling in Anterior Development of the Mammalian Embryo." Diss., 2013. http://hdl.handle.net/10161/7132.
Повний текст джерелаSonic hedgehog (Shh) is a critical secreted signaling molecule that regulates many aspects of organogenesis. In the absence of Shh, many organs, including the foregut, larynx, palate, cerebellum and heart do not form properly. However, the cellular details of the roles of Shh, including the relevant domains of Shh expression and reception, have not been elucidated for many of these processes.
The single embryonic foregut tube must divide into the trachea and esophagus, which does not occur in the Shh-null mutant. In Chapter 5, I use Cre-Lox technology to determine that the ventral foregut endoderm is the relevant source of Shh for this process and the mesoderm must directly receive that Shh signal. Surprisingly, this signaling event appears to occur two days before the foregut begins to divide, indicating an early essential role for Shh in foregut division.
Shh is also expressed at later stages in the maturing trachea and esophagus. In Chapter 6, I demonstrate that these domains serve to establish differentiated mesoderm. In the trachea, Shh from the endoderm signals directly to the mesoderm to form the tracheal cartilage rings. In the esophagus, the roles of Shh are more complex. Shh regulates the size of the esophagus and controls patterning of the concentric rings of esophageal mesoderm, however this process seems to be indirect, requiring autocrine Shh signaling within the esophageal endoderm.
The laryngeal apparatus is entirely absent in the Shh-null mouse. I n Chapter 3, I dissect the domains of Shh expression and reception required for laryngeal development and demonstrate that loss of endodermal Shh expression causes laryngotracheoesophageal clefts and malformed laryngeal cartilages. As much of laryngeal morphogenesis poorly understood, I also utilize dual mesodermal and neural crest fate maps to determine the embryonic origins of various laryngeal tissues. Finally, as Shh signaling often occurs in concert with Bone Morphogenic Protein (BMP) signaling, I investigate the roles of BMP signaling in laryngeal development.
Much of Shh signaling occurs at the primary cilium, to which Smoothened, a critical pathway member, must translocate upon Shh signal transduction. This process requires a Smo-Kif3a-βarretin complex in mammalian cell culture. However, the roles of βarrestins in mouse development, and their relationship to Shh signaling have not been investigated in vivo. To do so, in Chapter 4, I analyze the phenotypes of the βarr1/βarr2 double knockout embryos and demonstrate that they have palatal, cerebellar, cardiovascular and renal defects consistent with a specific impairment of mitogenic Shh signaling.
Altogether, my work dissects the cellular details of Shh signaling during multiple organ systems in the mouse embryo. I further analyze the consequences of absent or misregulated Shh signaling across multiple developmental contexts and determine that Shh plays critical and diverse roles in organogenesis.
Dissertation
Частини книг з теми "Beta arrestin signaling"
Yvinec, Romain, Mohammed Akli Ayoub, Francesco De Pascali, Pascale Crépieux, Eric Reiter, and Anne Poupon. "Workflow Description to Dynamically Model β-Arrestin Signaling Networks." In Beta-Arrestins, 195–215. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9158-7_13.
Повний текст джерелаUrs, Nikhil M. "Methods to Investigate the Role of β-Arrestin Signaling in Parkinson’s Disease." In Beta-Arrestins, 385–91. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9158-7_24.
Повний текст джерелаRosanò, Laura, Roberta Cianfrocca, and Anna Bagnato. "Methods to Investigate β-Arrestin-1/β-Catenin Signaling in Ovarian Cancer Cells." In Beta-Arrestins, 393–406. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9158-7_25.
Повний текст джерелаVirion, Zoé, Stefano Marullo, and Mathieu Coureuil. "Methods to Study the Roles of β-Arrestins in Meningococcal Signaling." In Beta-Arrestins, 325–34. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9158-7_20.
Повний текст джерелаLaporte, Stéphane A., and Mark G. H. Scott. "β-Arrestins: Multitask Scaffolds Orchestrating the Where and When in Cell Signalling." In Beta-Arrestins, 9–55. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9158-7_2.
Повний текст джерелаUrs, Nikhil M., Tanya L. Daigle, Jonathan Ting, and Marc G. Caron. "Targeting Beta-Arrestin Dependent Signaling in the Treatment of Parkinson’s Disease." In Catecholamine Research in the 21st Century, 103–4. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-800044-1.00090-8.
Повний текст джерелаТези доповідей конференцій з теми "Beta arrestin signaling"
Lin, Rui, David A. Zidar, and Julia K. L. Walker. "Beta-arrestin-2-dependent Signaling Promotes Th2 Cell CCR4-mediated Chemotaxis." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4049.
Повний текст джерелаSun, Jiyuan, Jingli Cai, and Yumei Feng. "Abstract B41: Inhibition of beta‐arrestin2‐CARMA3 signaling axis impairs lysophosphatidic acid‐induced ovarian cancer migration and invasion." In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Dec 6–9, 2009; Houston, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-09-b41.
Повний текст джерелаSun, Jiyuan, Jingli Cai, Yumei Feng, and Lei Guo. "Abstract 5286: Beta-arrestin2-CARMA3 signaling axis is required in lysophosphatidic acid-induced ovarian cancer migration and invasion." In 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.am10-5286.
Повний текст джерелаSun, Jiyuan, Jingli Cai, and Feng Yumei. "Abstract B22: Beta-arrestin2-CARMA3 signaling axis plays critical roles in lysophosphatidic acid-induced ovarian cancer migration and invasion." In Abstracts: AACR International Conference on Translational Cancer Medicine--; Mar 21–24, 2010; Amsterdam, The Netherlands. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1078-0432.tcme10-b22.
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