Academic literature on the topic 'Receptors, Death Domain'
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Journal articles on the topic "Receptors, Death Domain"
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Wajant, Harald. "Death receptors." Essays in Biochemistry 39 (October 1, 2003): 53–71. http://dx.doi.org/10.1042/bse0390053.
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Death receptors [Fas/Apo-1/CD95, TNF-R1 [tumour necrosis factor (TNF) receptor 1], DR3 [death receptor 3], TRAIL-R1 [TNF-related apoptosis-inducing ligand receptor 1], TRAIL-R2, DR6, p75-NGFR [p75-nerve growth factor receptor], EDAR [ectodermal dysplasia receptor]] form a subgroup of the TNF-R superfamily that can induce apoptosis (programmed cell death) via a conserved cytoplasmic signalling module termed the death domain. Although death receptors have been recognized mainly as apoptosis inducers, there is growing evidence that these receptors also fulfil a variety of nonapoptotic functions. This review is focused on the molecular mechanisms of apoptotic and non-apoptotic death receptor signalling in light of the phenotype of mice deficient in the various death receptors.
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Thomas, Lance R., Ronald L. Johnson, John C. Reed, and Andrew Thorburn. "The C-terminal Tails of Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL) and Fas Receptors Have Opposing Functions in Fas-associated Death Domain (FADD) Recruitment and Can Regulate Agonist-specific Mechanisms of Receptor Activation." Journal of Biological Chemistry 279, no. 50 (September 27, 2004): 52479–86. http://dx.doi.org/10.1074/jbc.m409578200.
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Members of the tumor necrosis factor (TNF) superfamily of receptors such as Fas/CD95 and the TNF-related apoptosis-inducing ligand (TRAIL) receptors DR4 and DR5 induce apoptosis by recruiting adaptor molecules and caspases. The central adaptor molecule for these receptors is a death domain-containing protein, FADD, which binds to the activated receptor via death domain-death domain interactions. Here, we show that in addition to the death domain, the C-terminal tails of DR4 and DR5 positively regulate FADD binding, caspase activation and apoptosis. In contrast, the corresponding region in the Fas receptor has the opposite effect and inhibits binding to the receptor death domain. Replacement of wild-type or mutant DR5 molecules into DR5-deficient BJAB cells indicates that some agonistic antibodies display an absolute requirement for the C-terminal tail for FADD binding and signaling while other antibodies can function in the absence of this mechanism. These data demonstrate that regions outside the death domains of DR4 and DR5 have opposite effects to that of Fas in regulating FADD recruitment and show that different death receptor agonists can use distinct molecular mechanisms to activate signaling from the same receptor.
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Foley, Caitlin J., Holly Freedman, Sheryl L. Choo, Christina Onyskiw, Nai Yang Fu, Victor C. Yu, Jack Tuszynski, Joanne C. Pratt, and Shairaz Baksh. "Dynamics of RASSF1A/MOAP-1 Association with Death Receptors." Molecular and Cellular Biology 28, no. 14 (May 12, 2008): 4520–35. http://dx.doi.org/10.1128/mcb.02011-07.
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ABSTRACT RASSF1A is a tumor suppressor protein involved in death receptor-dependent apoptosis utilizing the Bax-interacting protein MOAP-1 (previously referred to as MAP-1). However, the dynamics of death receptor recruitment of RASSF1A and MOAP-1 are still not understood. We have now detailed recruitment to death receptors (tumor necrosis factor receptor 1 [TNF-R1] and TRAIL-R1/DR4) and identified domains of RASSF1A and MOAP-1 that are required for death receptor interaction. Upon TNF-α stimulation, the C-terminal region of MOAP-1 associated with the death domain of TNF-R1; subsequently, RASSF1A was recruited to MOAP-1/TNF-R1 complexes. Prior to recruitment to TNF-R1/MOAP-1 complexes, RASSF1A homodimerization was lost. RASSF1A associated with the TNF-R1/MOAP-1 or TRAIL-R1/MOAP-1 complex via its N-terminal cysteine-rich (C1) domain containing a potential zinc finger binding motif. Importantly, TNF-R1 association domains on both MOAP-1 and RASSF1A were essential for death receptor-dependent apoptosis. The association of RASSF1A and MOAP-1 with death receptors involves an ordered recruitment to receptor complexes to promote cell death and inhibit tumor formation.
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Brojatsch, Jürgen, John Naughton, Heather B. Adkins, and John A. T. Young. "TVB Receptors for Cytopathic and Noncytopathic Subgroups of Avian Leukosis Viruses Are Functional Death Receptors." Journal of Virology 74, no. 24 (December 15, 2000): 11490–94. http://dx.doi.org/10.1128/jvi.74.24.11490-11494.2000.
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ABSTRACT The identification of TVBS3, a cellular receptor for the cytopathic subgroups B and D of avian leukosis virus (ALV-B and ALV-D), as a tumor necrosis factor receptor-related death receptor with a cytoplasmic death domain, provides a compelling argument that viral Env-receptor interactions are linked to cell death (4). However, other TVB proteins have been described that appear to have similar death domains but are cellular receptors for the noncytopathic subgroup E of ALV (ALV-E): TVBT, a turkey subgroup E-specific ALV receptor, and TVBS1, a chicken receptor for subgroups B, D, and E ALV. To begin to understand the role of TVB receptors in the cytopathic effects associated with infection by specific ALV subgroups, we asked whether binding of a soluble ALV-E surface envelope protein (SU) to its receptor can lead to cell death. Here we report that ALV-E SU-receptor interactions can induce apoptosis in quail or turkey cells. We also show directly that TVBS1and TVBT are functional death receptors that can trigger cell death by apoptosis via a mechanism involving their cytoplasmic death domains and activation of the caspase pathway. These data demonstrate that ALV-B and ALV-E use functional death receptors to enter cells, and it remains to be determined why only subgroups B and D viral infections lead specifically to cell death.
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Denecker, G., D. Vercammen, W. Declercq, and P. Vandenabeele. "Apoptotic and necrotic cell death induced by death domain receptors." Cellular and Molecular Life Sciences 58, no. 3 (March 2001): 356–70. http://dx.doi.org/10.1007/pl00000863.
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Varfolomeev, E. E., M. P. Boldin, T. M. Goncharov, and D. Wallach. "A potential mechanism of "cross-talk" between the p55 tumor necrosis factor receptor and Fas/APO1: proteins binding to the death domains of the two receptors also bind to each other." Journal of Experimental Medicine 183, no. 3 (March 1, 1996): 1271–75. http://dx.doi.org/10.1084/jem.183.3.1271.
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The p55 tumor necrosis factor (TNF) receptor and Fas/APO1 induce cell death via distinct regions in their intracellular domains. Three cytoplasmic proteins that bind to these receptor regions have been identified recently. One, MORT1 (also called FADD), binds to Fas/APO1 but not to p55-R; another, TRADD, binds to the p55 TNF receptor but not to Fas/APO1; and the third, RIP, binds weakly to both receptors. The regions within these proteins that are involved in binding to the receptors and the receptor regions to which they bind share a common sequence motif, that of the "death domain." This study shows that the death domain motifs in MORT1, TRADD, and RIP bind effectively to each other, a mode of binding that may allow "cross-talk" between the functional expression of the p55 TNF receptor and Fas/APO1.
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Gao, Yin, Xue Luan, Jacob Melamed, and Inka Brockhausen. "Role of Glycans on Key Cell Surface Receptors That Regulate Cell Proliferation and Cell Death." Cells 10, no. 5 (May 19, 2021): 1252. http://dx.doi.org/10.3390/cells10051252.
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Cells undergo proliferation and apoptosis, migration and differentiation via a number of cell surface receptors, most of which are heavily glycosylated. This review discusses receptor glycosylation and the known roles of glycans on the functions of receptors expressed in diverse cell types. We included growth factor receptors that have an intracellular tyrosine kinase domain, growth factor receptors that have a serine/threonine kinase domain, and cell-death-inducing receptors. N- and O-glycans have a wide range of functions including roles in receptor conformation, ligand binding, oligomerization, and activation of signaling cascades. A better understanding of these functions will enable control of cell survival and cell death in diseases such as cancer and in immune responses.
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Zhang, Xiaoxiao, Maud Bernoux, Adam R. Bentham, Toby E. Newman, Thomas Ve, Lachlan W. Casey, Tom M. Raaymakers, et al. "Multiple functional self-association interfaces in plant TIR domains." Proceedings of the National Academy of Sciences 114, no. 10 (February 3, 2017): E2046—E2052. http://dx.doi.org/10.1073/pnas.1621248114.
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The self-association of Toll/interleukin-1 receptor/resistance protein (TIR) domains has been implicated in signaling in plant and animal immunity receptors. Structure-based studies identified different TIR-domain dimerization interfaces required for signaling of the plant nucleotide-binding oligomerization domain-like receptors (NLRs) L6 from flax and disease resistance protein RPS4 fromArabidopsis. Here we show that the crystal structure of the TIR domain from theArabidopsisNLR suppressor of npr1-1, constitutive 1 (SNC1) contains both an L6-like interface involving helices αD and αE (DE interface) and an RPS4-like interface involving helices αA and αE (AE interface). Mutations in either the AE- or DE-interface region disrupt cell-death signaling activity of SNC1, L6, and RPS4 TIR domains and full-length L6 and RPS4. Self-association of L6 and RPS4 TIR domains is affected by mutations in either region, whereas only AE-interface mutations affect SNC1 TIR-domain self-association. We further show two similar interfaces in the crystal structure of the TIR domain from theArabidopsisNLR recognition ofPeronospora parasitica1 (RPP1). These data demonstrate that both the AE and DE self-association interfaces are simultaneously required for self-association and cell-death signaling in diverse plant NLRs.
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Essuman, Kow, Li Wan, Daniel W. Summers, Ryan G. Anderson, Yo Sasaki, Xianrong Mao, Aldrin Kay Yuen Yim, et al. "Redefining the TIR domain: From Axon Degeneration to Innate Immunity and Beyond." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 64.1. http://dx.doi.org/10.4049/jimmunol.202.supp.64.1.
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Abstract The Toll/Interleukin-1 Receptor (TIR) domain is an evolutionary ancient protein domain, present in numerous receptors and adaptor proteins, and is the signature-signaling domain of Toll-Like Receptors (TLRs). In animals, these TIR domains generally serve as scaffolds that promote the assembly of signaling complexes to trigger activation of pro-inflammatory cytokines and other defense-related products. In plants, TIR domain proteins are known to mediate disease resistance against pathogens, and trigger hypersensitive cell death. However, their mechanism of action has remained elusive. In bacteria, TIR domains have been associated with virulence and defense against some viruses. Here, we redefine the canonical scaffolding function of the TIR domain by showing that TIR domains can possess intrinsic enzymatic activity, and constitute a family of enzymes that cleave the essential metabolic cofactor Nicotinamide Adenine Dinucleotide (NAD+). We identify the TIR domain of SARM1 as the founding member of the TIR NADase family that triggers axon self-destruction upon axonal injury. We show that the TIR enzymatic activity in conserved in bacteria, and archaea, where in bacteria this NADase activity has recently been linked to defense against viruses. Finally, we extend our findings to plant innate immunity, and show that plant TIR-domain Immune Receptors trigger cell death and transduce recognition of pathogens into an immune response via this conserved enzymatic activity. Altogether, our findings establish TIR domain proteins as a new family of metabolic enzymes, and we posit that the scaffolding function in TLR signaling likely represents a repurposing of this evolutionary ancient enzymatic function.
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Thorburn, Jacqueline, Laura M. Bender, Michael J. Morgan, and Andrew Thorburn. "Caspase- and Serine Protease-dependent Apoptosis by the Death Domain of FADD in Normal Epithelial Cells." Molecular Biology of the Cell 14, no. 1 (January 2003): 67–77. http://dx.doi.org/10.1091/mbc.e02-04-0207.
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The adapter protein FADD consists of two protein interaction domains: a death domain and a death effector domain. The death domain binds to activated death receptors such as Fas, whereas the death effector domain binds to procaspase 8. An FADD mutant, which consists of only the death domain (FADD-DD), inhibits death receptor–induced apoptosis. FADD-DD can also activate a mechanistically distinct, cell type–specific apoptotic pathway that kills normal but not cancerous prostate epithelial cells. Here, we show that this apoptosis occurs through activation of caspases 9, 3, 6, and 7 and a serine protease. Simultaneous inhibition of caspases and serine proteases prevents FADD-DD–induced death. Inhibition of either pathway alone does not prevent cell death but does affect the morphology of the dying cells. Normal prostate epithelial cells require both the caspase and serine protease inhibitors to efficiently prevent apoptosis in response to TRAIL. In contrast, the serine protease inhibitor does not affect TRAIL-induced death in prostate tumor cells suggesting that the FADD-DD–dependent pathway can be activated by TRAIL. This apoptosis pathway is activated in a cell type–specific manner that is defective in cancer cells, suggesting that this pathway may be targeted during cancer development.
Dissertations / Theses on the topic "Receptors, Death Domain"
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Öberg, Camilla. "The life and death of the notch intracellular domain /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-464-X/.
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Wildsmith, G. C. "Structural and functional investigation of the cytoplasmic domain of the Fas death receptor." Thesis, University College London (University of London), 2015. http://discovery.ucl.ac.uk/1462353/.
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Activation of the transmembrane death receptor Fas (CD95/APO-1) by a membrane bound ligand (FasL/CD95L) activates the extrinsic pathway of apoptosis. Intracellular Fas death domains (DDs) are induced to oligomerise enabling binding to the adaptor protein FADD, thereby leading to the recruitment of procaspase 8 and other proteins to form the death inducing signalling complex (DISC).This thesis describes an investigation of the structure and function of the cytoplasmic Fas-DD. A model for the solution structure of the Fas-DD was published in 1996, it has since been reported that the death domain can form at least one other conformation when in complex with FADD. As a foundation to the work in this thesis, modern multidimensional NMR techniques have been used to solve the structure of the FasDD, to further probe the potential for alternative conformations. It has previously been reported that Fas can be phosphorylated at Tyr291, providing a platform for the recruitment of binding partners that can affect non-apoptotic signalling. The second part of this thesis details the development of an expressed protein ligation methodology to prepare a Tyr291 phosphorylated Fas DD to provide a basis for in vitro studies of the structural, dynamic and functional effects of phosphorylation. It is widely accepted that Fas is palmitoylated at Cys199 and recognised by the membrane cytoskeletal protein, ezrin. Fas palmitoylation is important for clathrinmediated internalisation of the DISC, and amplification of the caspase cascade. There are multiple reports detailing the binding of ezrin to Fas, but it is not clear whether this interaction occurs in a palmitoylation-dependent manner. Efforts to characterise an interaction between bacterially expressed intracellular Fas and ezrin proteins were carried out using a number of biophysical assays, described in the third part of this thesis. Building upon this, the fourth section explores the preparation of a palmitoylated Fas construct suitable for biophysical analysis by incubating recombinant Fas with palmitoyl-CoA.
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Park, Hyun Ho. "Structural and biochemical studies of cell death signaling /." Access full-text from WCMC:, 2007. http://proquest.umi.com/pqdweb?did=1428838901&sid=9&Fmt=2&clientId=8424&RQT=309&VName=PQD.
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Ferguson, Brian James. "Structural and biochemical analysis of the death domain complex formed at the Fas receptor." Thesis, University College London (University of London), 2005. http://discovery.ucl.ac.uk/1444407/.
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Fas (CD95) is a member of the death receptor superfamily of proteins that are involved in the initiation of apoptosis as induced by the binding of extracellular ligands. At present, little is known about the precise mechanism by which the signal initiated by the interaction between Fas ligand (FasL) and Fas is transduced across the cell membrane to start the apoptotic signalling cascade. The first step in this pathway is the recruitment of the Fas-associated death domain protein (FADD) to the cytoplasmic death domain of Fas via a homotypic protein/protein interaction. This binding event occurs after receptor ligation apparently without any post translational modification such as phosphorylation. In order to better understand this event we have investigated the interaction between the death domains of the human Fas and FADD proteins both in vitro and in a cellular context. The reported interaction between the Fas and FADD death domains (Fas-DD and FADD-DD) was recapitulated using the yeast 2-hybrid assay. Recombinant proteins were then produced for NMR spectroscopy experiments. FADD-DD is highly expressed, and easy to isolate soluble at physiological pH. This domain is readily expressed as a histidine tagged domain. Fas death domain expresses at low levels and produces soluble aggregates when concentrated at a pH above 4. However, it was found that using a Gbl fusion protein to express Fas-DD overcomes these problems and allowed the production of Fas-DD for NMR experiments. NMR titration experiments showed that when these two proteins interact a large, soluble complex is formed. This may be significant in relation to the increasing evidence for the importance of Fas-receptor clustering in its signalling. Mutational analysis of the Fas death domain was also carried out. Here, various previously described as well as several novel point mutations were made on the surface of the Fas death domain to investigate their effect on FADD-DD binding. These mutations were assayed using yeast 2-hybrid methods, NMR analysis and in a cell based assay. In the cell based assay wild type and mutant Fas receptors were overexpressed in a human cell line with no endogenous surface Fas expression. These cells were then assayed for their ability to undergo FasL-induced apoptosis. It was found that residues from many surface regions of Fas-DD are crucial for the FADD-DD interaction. This observation has potentially important implications for the nature of the organisation of the death domains in the death inducing signalling complex (DISC) formed at the Fas receptor.
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Jundi, Hala. "Elucidating ryanodine receptor domain interactions in sudden cardiac death : towards the development of novel therapeutic strategies." Thesis, Cardiff University, 2009. http://orca.cf.ac.uk/55106/.
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Interdomain Interactions within the complex three-dimensional architecture of the cardiac ryanodine receptor (RyR2) are pivotal in channel regulation. Acquired or genetic abnormalities that perturb these stabilising intra-molecular interactions are pathogenic. This laboratory identified the interacting- or l-Domain of human RyR2 that mediated interaction between cytoplasmic and transmembrane (TM) assemblies. To further elucidate the precise roles of functional motifs within the l-Domain, three contiguous fragments spanning RyR2 amino acid residues 3722-4610 were synthesised using a cell-free system. One fragment termed IDB (amino acid residues 4353-4499) profoundly modulated cellular Ca2+ cycling and resulted in the remarkable normalisation of intercellular synchrony following its microinjection into ouabain-treated cardiomyocyte monolayers. These phenomena were linked to IDB- mediated stabilisation of RyR2 and were fully corroborated using IDB purified from a bacterial expression system. Bioinformatic analysis revealed striking structural homology between sub-fragments of the RyR2 l-Domain and l-Domain-like regions of inositol 1,4,5- trisphosphate receptors (IP3R). Recombinant expression of l-domain sub-fragments in RyR- null human embryonic kidney (HEK) cells remodelled carbachol-evoked Ca2+-responses and suppressed homeostatic Ca2+ signalling events indicating that IDB also modulated IP3R signalling mechanisms. In both HL-1 and HEK cells, IDB-dependent Ca2+ modulation extended to surrounding cells that were not microinjected with recombinant protein. This so- called 'bystander effect' was mediated by the transfer of signalling molecules via direct cell- to-cell coupling (gap junctions) and also by the extracellular transmission of diffusible effectors. This thesis supports the concept that RyR2 stabilisation rescues pathogenic Ca2+ dysregulation and suggests that there is substantial merit in developing further epitope-targeting strategies for the therapeutic normalisation of Ca2+ cycling in cardiac disease.
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Mässenhausen, Anne von, Wulf Tonnus, and Andreas Linkermann. "Cell Death Pathways Drive Necroinflammation during Acute Kidney Injury." Karger, 2018. https://tud.qucosa.de/id/qucosa%3A71624.
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Renal tubules represent an intercellular unit and function as a syncytium. When acute tubular necrosis was first visualized to occur through a process of synchronized regulated necrosis (SRN) in handpicked primary renal tubules, it became obvious that SRN actually promotes nephron loss. This realization adds to our current understanding of acute kidney injury (AKI)-chronic kidney disease (CKD) transition and argues for the prevention of AKI episodes to prevent CKD progression. Because SRN is triggered by necroptosis and executed by ferroptosis, 2 recently identified signaling pathways of regulated necrosis, a combination therapy employing necrostatins and ferrostatins may be beneficial for protection against nephron loss. Clinical trials in AKI and during the process of kidney transplantation are now required to prevent SRN. Additionally, necrotic cell death drives autoimmunity and necroinflammation and therefore represents a therapeutic target even for the prevention of antibody-mediated rejection of allografts years after the transplantation process.
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Ermolaeva, Maria A. [Verfasser]. "Analysis of the physiological function of TNF receptor I associated death domain protein (TRADD) and familial cylindromatosis protein (CYLD) by using conditional gene targeting in mice / presented by Maria A. Ermolaeva." 2008. http://d-nb.info/991461797/34.
Full textBooks on the topic "Receptors, Death Domain"
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service), SpringerLink (Online, ed. Death receptors and cognate ligands in cancer. Heidelberg: Springer, 2009.
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Kalthoff, Holger. Death Receptors and Cognate Ligands in Cancer. Springer, 2012.
Find full textBook chapters on the topic "Receptors, Death Domain"
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Kahloula, Khaled, Djallal Eddine Houari Adli, Nadia Zouhairi, Kaddour Ziani, Miloud Slimani, Wafaa Arabi, Abdelmohcine Aimrane, et al. "Viral Infection of the Reproductive System in Times of COVID-19." In Research Anthology on Advancements in Women's Health and Reproductive Rights, 1–21. IGI Global, 2022. http://dx.doi.org/10.4018/978-1-6684-6299-7.ch001.
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Coronavirus (SARS-COV2) caused several deaths worldwide. This virus infects the target cell by binding to angiotensin-converting enzymes 2 (ACE2) receptor through its receptor-binding domain (RBD) and replicates. Thus, a high level of ACE2 expression is detected in the testicular cells so that the testis is believed to count as a potential target for direct damage by COVID-19. Moreover, the possibility of testicular damage may be caused by either direct viral invasion through interaction with ACE2 receptors or because of inflammatory response. Similarly, in women, literature reported the distribution and function of ACE2 in the female reproductive system, which is widely expressed in the ovary, uterus, vagina, and placenta. It regulates follicular development and ovulation, modulates luteal angiogenesis and degeneration, and influences regular changes in endometrial tissue and embryo development. Taking these functions into account, COVID-19 may disturb the female reproductive functions through regulating ACE2, resulting in infertility, menstrual disorder, and fetal distress.
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Kahloula, Khaled, Djallal Eddine Houari Adli, Nadia Zouhairi, Kaddour Ziani, Miloud Slimani, Wafaa Arabi, Abdelmohcine Aimrane, et al. "Viral Infection of the Reproductive System in Times of COVID-19." In Handbook of Research on Pathophysiology and Strategies for the Management of COVID-19, 176–96. IGI Global, 2022. http://dx.doi.org/10.4018/978-1-7998-8225-1.ch011.
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Coronavirus (SARS-COV2) caused several deaths worldwide. This virus infects the target cell by binding to angiotensin-converting enzymes 2 (ACE2) receptor through its receptor-binding domain (RBD) and replicates. Thus, a high level of ACE2 expression is detected in the testicular cells so that the testis is believed to count as a potential target for direct damage by COVID-19. Moreover, the possibility of testicular damage may be caused by either direct viral invasion through interaction with ACE2 receptors or because of inflammatory response. Similarly, in women, literature reported the distribution and function of ACE2 in the female reproductive system, which is widely expressed in the ovary, uterus, vagina, and placenta. It regulates follicular development and ovulation, modulates luteal angiogenesis and degeneration, and influences regular changes in endometrial tissue and embryo development. Taking these functions into account, COVID-19 may disturb the female reproductive functions through regulating ACE2, resulting in infertility, menstrual disorder, and fetal distress.
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"TRADD (tumor necrosis factor receptor associated death domain)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 1987. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_17158.
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Coulson, E. J., K. Reid, K. M. Shipham, S. Morley, T. J. Kilpatrick, and P. F. Bartlett. "The role of neurotransmission and the Chopper domain in p75 neurotrophin receptor death signaling." In Progress in Brain Research, 41–62. Elsevier, 2004. http://dx.doi.org/10.1016/s0079-6123(03)46003-2.
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Kim, Dong Hoon. "Colonial Film Spectatorship: Nationalist Enough?" In Eclipsed Cinema. Edinburgh University Press, 2017. http://dx.doi.org/10.3366/edinburgh/9781474421805.003.0005.
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In the last two chapters, my critical and historiographical concerns draw on theories of film spectatorship and reception in order to further extend the topography of Joseon cinema. The forth chapter considers film-viewing as a political domain in which various forms of colonial tensions were represented and mediated. Taking the dearth of local productions and the predominance of Hollywood productions into consideration, the author argues any attempt to limit Korean spectators’ movie-going and film-viewing patterns only to Joseon films is bound to be a reductionist understanding of Joseon film culture. Thus, the chapter explores the issues in colonial spectatorship in relation to not only local but imported films. It focuses particularly on how Korean spectators’ engagement with American films emerged as the main subject of political tensions and hegemonic struggles with regard to the colonial situation, detailing a variety of receptions and interpretations of the dominance of Hollywood film in the Joseon film.
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Kumar, Vijay. "Learning from Bats to Escape from Potent or Severe Viral Infections." In Origin and Impact of COVID-19 Pandemic Originating From SARS-CoV-2 Infection Across the Globe [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.98916.
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The COVID-19 pandemic that started in December 2019 in Wuhan city, China has created chaos all over the world with over 185 million infection cases and 4 million deaths world-wide. The pathogen behind COVID-19 has been identified as severe acute respiratory syndrome Coronavirus 2 (SARS-CoV-2) that is more close to the previous SARS-CoV responsible for SARS epidemic 2002–2003. Although, SARS-CoV-2 also differs from SARS-CoV in many aspects as indicated by genetic studies. For example, SARS-CoV does not have a furin binding domain or site, whereas its presence in SARS-CoV-2 spike (S) protein increases its potential for infectivity. The horseshoe bats (Rhinolphus species) from China are considered as primary animal reservoirs for SARS-CoV and SARS-CoV-2. However, along with CoVs, bats also harbor many other viral pathogens (Ebola, Nipah, and Hendra viruses) without having serious infections. The bat physiology plays a crucial role in harboring these viruses along with adaptations to longevity and slow aging process. The immune system plays a crucial role in the clearance or establishment of the infection. Present chapter discusses different immunological aspects (innate immune response comprising the virus recognizing pattern recognition receptors (PRRs), type 1 interferon production, pro- and anti-inflammatory immune response, and adaptive immune response) that help bats to control viral infection without getting a severe infection as compared to other mammals, including humans.
Conference papers on the topic "Receptors, Death Domain"
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Haferkamp, Bonnie, Yuting Lin, Brad Godfrey, and Jialing Xiang. "Abstract 4539: Androgen receptor N-term death domains induce apoptosis through a bax-mediated mitochondrial pathway." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4539.
Full textReports on the topic "Receptors, Death Domain"
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Sessa, Guido, and Gregory Martin. role of FLS3 and BSK830 in pattern-triggered immunity in tomato. United States Department of Agriculture, January 2016. http://dx.doi.org/10.32747/2016.7604270.bard.
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Pattern-recognition receptors (PRRs) located on the plant cell surface initiate immune responses by perceiving conserved pathogen molecules known as pathogen-associated molecular patterns (PAMPs). PRRs typically function in multiprotein complexes that include transmembrane and cytoplasmickinases and contribute to the initiation and signaling of pattern-triggered immunity (PTI). An important challenge is to identify molecular components of PRR complexes and downstream signaling pathways, and to understand the molecular mechanisms that mediate their function. In research activities supported by BARD-4931, we studied the role of the FLAGELLIN SENSING 3 (FLS3) PRR in the response of tomato leaves to flagellin-derivedPAMPs and PTI. In addition, we investigated molecular properties of the tomato brassinosteroid signaling kinase 830 (BSK830) that physically interacts with FLS3 and is a candidate for acting in the FLS3 signaling pathway. Our investigation refers to the proposal original objectives that were to: 1) Investigate the role of FLS3 and its interacting proteins in PTI; 2) Investigate the role of BSK830 in PTI; 3) Examine molecular and phosphorylation dynamics of the FLS3-BSK830 interaction; 4) Examine the possible interaction of FLS3 and BSK830 with Pstand Xcveffectors. We used CRISPR/Cas9 techniques to develop plants carrying single or combined mutations in the FLS3 gene and in the paralogsFLS2.1 and FLS2.2 genes, which encode the receptor FLAGELLIN SENSING2 (FLS2), and analyzed their function in PTI. Domain swapping analysis of the FLS2 and FLS3 receptors revealed domains of the proteins responsible for PAMP detection and for the different ROS response initiated by flgII-28/FLS3 as compared to flg22/FLS2. In addition, in vitro kinase assays and point mutations analysis identified FLS2 and FLS3 domains required for kinase activity and ATP binding. In research activities on tomato BSK830, we found that it interacts with PRRs and with the co-receptor SERK3A and PAMP treatment affects part of these interactions. CRISPR/Cas9 bsk830 mutant plants displayed enhanced pathogen susceptibility and reduced ROS production upon PAMP treatment. In addition, BSK830 interacted with 8 Xanthomonastype III secreted effectors. Follow up analysis revealed that among these effectors XopAE is part of an operon, is translocated into plant cells, and displays E3 ubiquitinligase activity. Our investigation was also extended to other Arabidopsis and tomato BSK family members. Arabidopsis BSK5 localized to the plant cell periphery, interacted with receptor-like kinases, and it was phosphorylatedin vitro by the PEPR1 and EFRPRRs. bsk5 mutant plants displayed enhanced susceptibility to pathogens and were impaired in several, but not all, PAMP-induced responses. Conversely, BSK5 overexpression conferred enhanced disease resistance and caused stronger PTI responses. Genetic complementation suggested that proper localization, kinase activity, and phosphorylation by PRRs are critical for BSK5 function. BSK7 and BSK8 specifically interacted with the FLS2 PRR, their respective mutant plants were more susceptible to B. cinereaand displayed reduced flg22-induced responses. The tomato BSK Mai1 was found to interact with the M3KMAPKKK, which is involved in activation of cell death associated with effector-triggered immunity. Silencing of Mai1 in N. benthamianaplants compromised cell death induced by a specific class of immune receptors. In addition, co-expression of Mai1 and M3Kin leaves enhanced MAPKphosphorylation and cell death, suggesting that Mai1 acts as a molecular link between pathogen recognition and MAPK signaling. Finally, We identified the PP2C phosphatase Pic1 that acts as a negative regulator of PTI by interacting with and dephosphorylating the receptor-like cytoplasmickinase Pti1, which is a positive regulator of plant immunity. The results of this investigation shed new light on the molecular characteristics and interactions of components of the immune system of crop plants providing new knowledge and tools for development of novel strategies for disease control.
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Coplin, David L., Shulamit Manulis, and Isaac Barash. roles Hrp-dependent effector proteins and hrp gene regulation as determinants of virulence and host-specificity in Erwinia stewartii and E. herbicola pvs. gypsophilae and betae. United States Department of Agriculture, June 2005. http://dx.doi.org/10.32747/2005.7587216.bard.
Full textAbstract:
Gram-negative plant pathogenic bacteria employ specialized type-III secretion systems (TTSS) to deliver an arsenal of pathogenicity proteins directly into host cells. These secretion systems are encoded by hrp genes (for hypersensitive response and pathogenicity) and the effector proteins by so-called dsp or avr genes. The functions of effectors are to enable bacterial multiplication by damaging host cells and/or by blocking host defenses. We characterized essential hrp gene clusters in the Stewart's Wilt of maize pathogen, Pantoea stewartii subsp. stewartii (Pnss; formerly Erwinia stewartii) and the gall-forming bacterium, Pantoea agglomerans (formerly Erwinia herbicola) pvs. gypsophilae (Pag) and betae (Pab). We proposed that the virulence and host specificity of these pathogens is a function of a) the perception of specific host signals resulting in bacterial hrp gene expression and b) the action of specialized signal proteins (i.e. Hrp effectors) delivered into the plant cell. The specific objectives of the proposal were: 1) How is the expression of the hrp and effector genes regulated in response to host cell contact and the apoplastic environment? 2) What additional effector proteins are involved in pathogenicity? 3) Do the presently known Pantoea effector proteins enter host cells? 4) What host proteins interact with these effectors? We characterized the components of the hrp regulatory cascade (HrpXY ->7 HrpS ->7 HrpL ->7 hrp promoters), showed that they are conserved in both Pnss and Fag, and discovered that the regulation of the hrpS promoter (hrpSp) may be a key point in integrating apoplastic signals. We also analyzed the promoters recognized by HrpL and demonstrated the relationship between their composition and efficiency. Moreover, we showed that promoter strength can influence disease expression. In Pnss, we found that the HrpXY two-component signal system may sense the metabolic status of the bacterium and is required for full hrp gene expression in planta. In both species, acyl-homoserine lactone-mediated quorum sensing may also regulate epiphytic fitness and/or pathogenicity. A common Hrp effector protein, DspE/WtsE, is conserved and required for virulence of both species. When introduced into corn cells, Pnss WtsE protein caused water-soaked lesions. In other plants, it either caused cell death or acted as an Avr determinant. Using a yeast- two-hybrid system, WtsE was shown to interact with a number of maize signal transduction proteins that are likely to have roles in either programmed cell death or disease resistance. In Pag and Pab, we have characterized the effector proteins HsvG, HsvB and PthG. HsvG and HsvB are homologous proteins that determine host specificity of Pag and Pab on gypsophila and beet, respectively. Both possess a transcriptional activation domain that functions in yeast. PthG was found to act as an Avr determinant on multiple beet species, but was required for virulence on gypsophila. In addition, we demonstrated that PthG acts within the host cell. Additional effector genes have been characterized on the pathogenicity plasmid, pPATHₚₐg, in Pag. A screen for HrpL- regulated genes in Pnsspointed up 18 candidate effector proteins and four of these were required for full virulence. It is now well established that the virulence of Gram-negative plant pathogenic bacteria is governed by Hrp-dependent effector proteins. However; the mode of action of many effectors is still unresolved. This BARD supported research will significantly contribute to the understanding of how Hrp effectors operate in Pantoea spp. and how they control host specificity and affect symptom production. This may lead to novel approaches for genetically engineering plants resistant to a wide range of bacterial pathogens by inactivating the Hrp effectors with "plantabodies" or modifying their receptors, thereby blocking the induction of the susceptible response. Alternatively, innovative technologies could be used to interfere with the Hrp regulatory cascade by blocking a critical step or mimicking plant or quorum sensing signals.
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Sessa, Guido, and Gregory B. Martin. molecular link from PAMP perception to a MAPK cascade associated with tomato disease resistance. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7597918.bard.
Full textAbstract:
The research problem: The detection of pathogen-associated molecular patterns (PAMPs) by plant pattern recognition receptors (PRRs) is a key mechanism by which plants activate an effective immune response against pathogen attack. MAPK cascades are important signaling components downstream of PRRs that transduce the PAMP signal to activate various defense responses. Preliminary experiments suggested that the receptor-like cytoplasmickinase (RLCK) Mai5 plays a positive role in pattern-triggered immunity (PTI) and interacts with the MAPKKK M3Kε. We thus hypothesized that Mai5, as other RLCKs, functions as a component PRR complexes and acts as a molecular link between PAMP perception and activation of MAPK cascades. Original goals: The central goal of this research was to investigate the molecular mechanisms by which Mai5 and M3Kε regulate plant immunity. Specific objectives were to: 1. Determine the spectrum of PAMPs whose perception is transmitted by M3Kε; 2. Identify plant proteins that act downstream of M3Kε to mediate PTI; 3. Investigate how and where Mai5 interacts with M3Kε in the plant cell; 4. Examine the mechanism by which Mai5 contributes to PTI. Changes in research directions: We did not find convincing evidence for the involvement of M3Kε in PTI signaling and substituted objectives 1 and 3 with research activities aimed at the analysis of transcriptomic profiles of tomato plants during the onset of plant immunity, isolation of the novel tomato PRR FLS3, and investigation of the involvement of the RLCKBSKs in PTI. Main achievements during this research program are in the following major areas: 1. Functional characterization of Mai5. The function of Mai5 in PTI signaling was demonstrated by testing the effect of silencing the Mai5 gene by virus-induced gene silencing (VIGS) experiments and in cell death assays. Domains of Mai5 that interact with MAPKKKs and subcellular localization of Mai5 were analyzed in detail. 2. Analysis of transcriptional profiles during the tomato immune responses to Pseudomonas syringae (Pombo et al., 2014). We identified tomato genes whose expression is induced specifically in PTI or in effector-triggered immunity (ETI). Thirty ETI-specific genes were examined by VIGS for their involvement in immunity and the MAPKKK EPK1, was found to be required for ETI. 3. Dissection of MAP kinase cascades downstream of M3Kε (Oh et al., 2013; Teper et al., 2015). We identified genes that encode positive (SGT and EDS1) and negative (WRKY1 and WRKY2) regulators of the ETI-associated cell death mediated by M3Kε. In addition, the MKK2 MAPKK, which acts downstream of M3Kε, was found to interact with the MPK3 MAPK and specific MPK3 amino acids involved interaction were identified and found to be required for induction of cell death. We also identified 5 type III effectors of the bacterial pathogen Xanthomonaseuvesicatoria that inhibited cell death induced by components of ETI-associated MAP kinase cascades. 4. Isolation of the tomato PRR FLS3 (Hind et al., submitted). FLS3, a novel PRR of the LRR-RLK family that specifically recognizes the flagellinepitope flgII-28 was isolated. FLS3 was shown to bind flgII-28, to require kinase activity for function, to act in concert with BAK1, and to enhance disease resistance to Pseudomonas syringae. 5. Functional analysis of RLCKs of the brassinosteroid signaling kinase (BSK) family.Arabidopsis and tomato BSKs were found to interact with PRRs. In addition, certain ArabidospsisBSK mutants were found to be impaired in PAMP-induced resistance to Pseudomonas syringae. Scientific and agricultural significance: Our research activities discovered and characterized new molecular components of signaling pathways mediating recognition of invading pathogens and activation of immune responses against them. Increased understanding of molecular mechanisms of immunity will allow them to be manipulated by both molecular breeding and genetic engineering to produce plants with enhanced natural defense against disease.