Auswahl der wissenschaftlichen Literatur zum Thema „Protéine contenant un domaine BEACH“
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Dissertationen zum Thema "Protéine contenant un domaine BEACH"
Delage, Laure. „Des déficiences génétiques comme modèles naturels pour l'étude de la régulation des checkpoints immunitaires et la caractérisation des réponses auto-immunes“. Electronic Thesis or Diss., Université Paris Cité, 2021. http://www.theses.fr/2021UNIP5190.
Der volle Inhalt der QuelleRecessive NBEAL2 mutations have been reported in patients with Gray Platelet Syndrome (GPS). This syndrome is characterized by a macro-thrombocytopenia, with platelets lacking alpha-granules, leading to bleeding disorders, often associated with splenomegaly. Thus, NBEAL2 plays a crucial role in the trafficking of alpha-granules in platelets. Moreover, our lab has also described NBEAL2 deficiencies in patients presenting clinical features of the autoimmune lymphoproliferative syndrome, suggesting a role of NBEAL2 in immune homeostasis and tolerance. A broader international cohort of GPS patients has been described, revealing immune system abnormalities (autoimmune diseases, autoantibodies, lymphopenia). If the role of NBEAL2 in the traffic of granules is often investigated, the exact mechanism leading to the development of autoimmune manifestations in GPS patients remains unknown. NBEAL2 belongs to a protein family involved in vesicular trafficking, all of which possess a conserved BEACH domain. Within this BEACH-domain containing proteins family, one of the closest members to NBEAL2 is LRBA. LRBA is involved in the recycling of CTLA-4, an inhibitory immune checkpoint. CTLA-4 plays a crucial role in the regulation of immune responses and tolerance. Recessive mutations of LRBA lead to similar clinical features as partial CTLA-4 deficiency: autoimmunity, lymphocytic infiltrations, and progressive B lymphopenia. Physiologically, LRBA prevents the lysosomal degradation of CTLA-4 and allows its recycling to the membrane. By analogy with LRBA, we investigated the importance of NBEAL2 in immune checkpoints intracellular trafficking and we brought new insights on its role in lymphocytes. Thus, NBEAL2 is a scaffold protein, binding LRBA, and involved in CTLA-4 trafficking as well as in vesicular trafficking in general. This work brings new knowledge to the regulation of CTLA-4 in activated T lymphocytes, a list of new partners for NBEAL2 protein and a new model of vesicular trafficking in which NBEAL2 is involved. Finally, a better understanding of the mechanisms leading to autoimmunity in patients with gray platelets syndrome could lead to better diagnosis and treatment management
Bauer, Florian Franz. „Etude d'un mutant de Saccharomyces cerevisiae présentant une viabilité réduite en conditions de carence : caractérisation d'une protéine contenant un domaine SH3“. Bordeaux 2, 1992. http://www.theses.fr/1992BOR28208.
Der volle Inhalt der QuelleThebault, Sabine. „Caractérisation d'une nouvelle protéine humaine contenant un domaine homologue à l'I-mfa : implication dans la régulation de l'expression de deux rétrovirus humains, HTLV-I et HIV-1“. Montpellier 1, 2000. http://www.theses.fr/2000MON1T013.
Der volle Inhalt der QuelleMartinat, Charlotte. „Rôle de la sumoylation dans les activités de SAMHD1, un facteur de restriction du VIH-1 dans les cellules non cyclantes“. Thesis, Sorbonne Paris Cité, 2018. http://www.theses.fr/2018USPCC246.
Der volle Inhalt der QuelleSince its discovery seven years ago, SAMHD1 has emerged as an important cellular factor that limits the replication of the Human immunodeficiency virus type 1 (HIV-1) at the reverse transcription step in non-cycling immune cells. HIV-2 and some SIV overcome this restriction by encoding the Vpx protein, which bridges SAMHD1 to the proteasomal degradation pathway. A wealth of experimental evidence indicates that SAMHD1 triphosphohydrolase (dNTPAse) activity, which is responsible for cellular dNTP pools depletion, accounts for the premature termination of viral replication. Notably, SAMHD1 expression is not sufficient to render any tested cell type resistant to HIV-1. Besides, there is no strict link between SAMHD1 capacity to deplete dNTP pools and its neutralizing function. Phosphorylation of residue T592 is proposed to downregulate the antiviral function of SAMHD1 in cycling cells. However, the analysis of phosphomimetic or unphosphorytable mutants of SAMHD1 leads to contradictory results. Altogether, these data suggest that SAMHD1-mediated restriction may neither exclusively rely on its dNTPase activity, nor solely depend on the phosphorylation status of T592.We have demonstrated that SAMHD1 undergoes SUMOylation, i.e. a post-translational modification consisting in the reversible conjugation of SUMO on a target protein; and have identified the major sites of modification. Our results show that mutations preventing SAMHD1 SUMOylation, in particular at residue K595 that lies close to the phosphorytable T592 site, inhibit its antiviral properties without impairing its dNTPase activity. Notably, an analogous phenotype is observed upon deletion of SAMHD1 C-terminus (Δ595-626). Based on these data, we speculate that phosphorytable T592 and SUMOylated K595 residues are part of an interface in SAMHD1 C-terminal tail that is responsible for the recruitment of still unknown cofactor(s) involved in the mechanism of HIV-1 infection restriction. Our work highlights a novel aspect of SAMHD1 regulation and participates to the characterization of molecular basis underlying its antiviral function. The identification of one or several cellular partners will allow a better understanding of retroviral restriction mechanism and could serve as new therapeutic targets to fight HIV-1 infection
Martine, Pierre. „Le rôle d'HSP70 sur l'activation de l'inflammasome NLRP3“. Thesis, Bourgogne Franche-Comté, 2017. http://www.theses.fr/2017UBFCI007.
Der volle Inhalt der QuelleNLRP3 inflammasome is a multi-protein complex aimed at producing IL-1β in response to danger signals. Gain of function mutations of NLRP3 are responsible for inflammatory diseases, so NLRP3-dependent inflammation required tight regulation. Here we investigated the importance of the stress sensor, Heat Shock Protein 70 (HSP70) on the NLRP3 inflammasome activation. First, the lack of HSP70 leads to a worsening of NLRP3-dependent peritonitis in mice. HSP70 deficiency also enhances caspase-1 activation and IL-1β production by murine Bone Marrow-Derived Macrophages (BMDMs) under NLRP3 activators treatment in vitro. These phenomena are associated with an increase in the number and size of ASC/NLRP3 specks. At the opposite side, the overexpression of HSP70 in BMDMs decreases caspase-1 activation and IL-1β production under NLRP3 activators treatment in vitro. One possible explanation of the inhibitory effect of HSP70 is its interaction with NLRP3. A heat shock, used as a way to induce the expression of HSP70 also inhibits the NLRP3 inflammasome activation in vitro. Finally, in vivo hyperthermia also inhibits peritonitis features in mice, highlighting the physiological relevance of our observations. This study provides evidences on the inhibitory role of HSP70 on the NLRP3 inflammasome and on the possibility to treat inflammatory diseases by inducing its expression, mainly by hyperthermia
Zecchin, Mathilde. „Le rôle du récepteur nucléaire Rev-erb-α dans les maladies inflammatoires : la régulation circadienne du complexe inflammasome NLRP3 dans l'hépatite fulminante et l'inhibition du développement de l'athérosclérose et de la calcification vasculaire“. Thesis, Lille, 2018. http://www.theses.fr/2018LILUS057.
Der volle Inhalt der QuelleAtherosclerosis is chronic inflammatory disease of the vascular wall, which consists inthe accumulation of Low Density Lipoproteins (LDL) into the vascular wall triggering theinternalization of leucocytes. Recruited monocytes differentiate into macrophages to removeLDL through the so-called reverse cholesterol transport pathway. However, when flux isimpaired, lipid-laden macrophages become foam cells leading to their apoptosis or necrosis.Their lipid content and cellular debris are then released in the extracellular matrix, thus formingthe necrotic core. In addition, laden-cholesterol crystals trigger lysosomal damage inmacrophage, which activates the NLRP3 inflammasome complex. NLRP3 inflammasome isinvolved in the maturation of the pro-caspase 1, which subsequently cleaves the pro- IL1B andpro-IL18 into mature IL1B and IL18. These interleukins are then released and stimulate thesecretion of interferon γ by CD4+ T cells, leading to the proliferation and the migration ofSmooth Muscle Cells (SMC) toward the necrotic core to form the fibrous cap. In addition tothe numerous risk factors of cardiovascular diseases such as diabetes or smoking, disruption ofdaily rhythms, as seen in shiftwork, increases the incidence of these diseases. Beyond its majorrole in metabolism and inflammation control, the nuclear receptor Rev-erb-α is also a corecomponent of the molecular clock. Altogether, it thus represents a putative therapeutic target inthe treatment of such multifactorial diseases related to clock impairment. My work shows thatthe deletion of Rev-erbα in a murine model of atherosclerosis (LDLr-/-) leads to an increase inplasma lipid levels and accelerates atherogenesis. In addition, Rev-erb-α regulates the circadianexpression of the NLRP3 pathway components as well as the subsequent secretion of IL1B andIL18 in primary human and mouse macrophages. At the molecular level, Rev-erb-α directlyrepresses the NLRP3 pathway, whereas Rev-erbα deficiency enhances its activation. Thismechanism may regulate the circadian susceptibility to inflammatory stimuli depending on thetime of challenge in acute inflammation models such as fulminant hepatitis or peritonitis. Theabsence of Rev-erbα also induces the expression of Nlrp3, Il1β and Il18 in models of chronicinflammation such as atherosclerosis as well as the expression of NLRP3 in lesionalmacrophages. In addition, IL1B and IL18 stimulate the differentiation of SMCs into osteoblastlikecells that form intimal calcification. It is noteworthy that Rev-erbα deletion in LDLr-/- miceis associated to an increase in lesion calcification in vivo, while the absence of Rev-erb-α inprimary SMCs increases their differentiation into osteoblasts and the formation of calciumdeposit in vitro. Interestingly, this differential effect observed on calcium deposition in vitro isexacerbated when primary SMCs are stimulated in culture with IL1B. Therefore, Rev-erb-α may be involved not only in macrophage-mediated IL1B production but also in the sensing ofsuch signal by SMCs. Conversely, treatment with Rev-erb ligands inhibits these effects. Thiswork emphasizes the key role of Rev-erb-α in the circadian regulation of the inflammatoryresponse and in the development of cardiovascular diseases, thus identifying Rev-erb-α as anew therapeutic target that act on several aspects of the pathology