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Artykuły w czasopismach na temat "Récepteurs nucléaires à l'Acide Rétinoïque"
Mark, Manuel, i Pierre Chambon. "Récepteurs de l'acide rétinoïque et morphogenèse". Annales de l'Institut Pasteur / Actualités 8, nr 1 (kwiecień 1997): 85–95. http://dx.doi.org/10.1016/s0924-4204(97)83336-7.
Pełny tekst źródłaCavaillès, V. "N-CoR et SMRT sont des corépresseurs transcriptionnels des récepteurs des hormones thyroïdiennes et de l'acide rétinoïque." médecine/sciences 12, nr 2 (1996): 234. http://dx.doi.org/10.4267/10608/721.
Pełny tekst źródłaDejean, Anne. "Les récepteurs nucléaires de l’acide rétinoïque : une base moléculaire commune pour le cancer du foie et les leucémies aiguës promyélocytaires". Bulletin de l'Académie Nationale de Médecine 186, nr 4 (kwiecień 2002): 751–57. http://dx.doi.org/10.1016/s0001-4079(19)34295-5.
Pełny tekst źródłaKahn, A. "Les récepteurs RXR sont des co-régulateurs des gènes répondant à l'acide rétinoïque, aux hormones thyroïdiennes et à la vitamine D". médecine/sciences 8, nr 3 (1992): 283. http://dx.doi.org/10.4267/10608/3121.
Pełny tekst źródłaRedormet, Anabelle, Catherine Noel-Suberville, Stéphane Bonilla, Rachel Groubet i Paul Higueret. "Effets d’un régime hyperlipidique sur l’expression des récepteurs nucléaires de l’acide rétinoïque (P-MRs), de la triiodothyronine (TRs) et des proliférateurs de peroxisomes (PPARs) dans le foie de rat". Oléagineux, Corps gras, Lipides 7, nr 1 (styczeń 2000): 107–8. http://dx.doi.org/10.1051/ocl.2000.0107.
Pełny tekst źródłaRozprawy doktorskie na temat "Récepteurs nucléaires à l'Acide Rétinoïque"
Mouchon, Arnaud. "Modulation de l'activité des récepteurs à l'acide rétinoïque par des interactions moléculaires". Lille 1, 1999. https://pepite-depot.univ-lille.fr/LIBRE/Th_Num/1999/50376-1999-191.pdf.
Pełny tekst źródłaL'ensemble des résultats obtenus par la suite identifie la région 403-410 comme essentielle pour l'activité biologique du récepteur, pour la liaison aux ligands, pour le recrutement des co-activateurs ou co-répresseur et de ce fait, essentielle dans l'interprétation de la pharmacologie des rétinoïdes (B. Lefebvre et al. , Mol. Cell. Endocrinol 1998a ; B. Lefebvre et al. , Biochemistry 1998b). Nous avons enfin montré que la capacité des ligands naturels et synthétiques à induire l'activité transcriptionnelle d'un gène chimérique est proportionnelle à leur capacité à recruter le co-activateur SRC1. Outre la structure du ligand, nous avons observé que l'ADN et le RXR exerçaient des régulations allostériques sur ces interactions protéines-protéines (A. Mouchon et al. , Mol. Cell. Biol. 1999). L'ensemble de ces résultats identifie la région 403-410 du hRAR[alpha] comme essentielle pour l'activité biologique du récepteur, par son implication dans la liaison et l'interprétation de la pharmacologie des ligands ; de plus, la structure du ligand a un effet considérable sur les transitions de structure que subit le RAR dans le contexte de l'hétérodimère lié à l'ADN, structure qui est également modulée par la structure du RARE et vraisemblablement par RXR
Martin, Perrine. "Recherche de nouveaux partenaires protéiques du Récepteur de l'Acide Rétinoïque : étude des interactions RAR-PLZF et RAR-PCNA". Lille 2, 2005. http://www.theses.fr/2005LIL2S003.
Pełny tekst źródłaThe Retinoic Acid Receptors (RAR) interact, in a ligand-dependent manner, with many coregulators which are involved in a broad spectrum of biological responses, from embryonic development to cell growth control. The transactivation function of these ligand-inducible transcription factors resides mainly, but not exclusively, in their Ligand Binding Domain (AF2) which recruits or dissociates coregulators in a ligand-dependent manner. Nevertheless, the RAR AF2-independent functions are not much elucidated. In this study, we have identified, by yeast two-hybrid screen, new RARa two partners, the PLZF (Promyelocytic Leukemia Zinc Finger) and PCNA (Proliferating Cell Nuclear Antigen) proteins. These two proteins interact physically and functionally with the RARa and act as RARa repressors. In addition, they have very distinct functions and exert their repressor effect through different domains and via different mechanisms. We have demonstrated that PLZF interferes probably with RAR-RXR dimerization. In contrast, PCNA interacts with RAR-RXR heterodimer bound to its response element and represses its transcriptional activity in a promoter- and cell-specific manner. These observations demonstrate new mechanisms by which RARa activity is controlled, and suggest a link between RARa, embryonic development and hematopoiesis in the case of PLZF and between RARa, cell cycle and DNA repair in the case of PCNA
Lalevée, Sébastien. "Les récepteurs nucléaires de l’acide rétinoïque : phosphorylation et contrôle dynamique de l’association-dissociation de complexes protéiques". Strasbourg, 2009. https://publication-theses.unistra.fr/public/theses_doctorat/2009/LALEVEE_Sebastien_2009.pdf.
Pełny tekst źródłaThe effects of Retinoids (active derivatives of Vitamin A) are mediated by two families of nuclear receptors, RAR (α, β and γ) and RXR (α, β and γ). In vivo, the RA signal is transmitted by RAR/RXR heterodimers, which function as ligand‐dependent transcriptional regulators and bind to RARE (Retinoic Acid Response Element) at the promoters of target genes. Our team demonstrated that two domains of RARs, the NTD (N‐terminal Domain) and the LBD (Ligand Binding Domain), are targets for phosphorylation processes that control RAR transcription. In order to decipher how phosphorylation controls RARs functions, I analyzed the dynamics of RAR (α and γ) association/dissociation with different protein partners depending on RARs phosphorylation state. In the case of RARα, I highlighted the consequences of LBD phosphorylation at serine 369, localized in close vicinity to the cyclin H docking site. This phosphorylation, via conformational changes, influences the recruitment of cyclin H associated to the cdk7 kinase of the general transcription factor TFIIH. This effect is at the basis of a cascade leading to the phosphorylation of the NTD by cdk7. I also participated to the study of another RARα partner, SUG‐1, a subunit of the proteasome. SUG‐1 plays a dual role in RARα target gene transcription by regulating the dynamic of transcription without proteolysis and by signaling the end of the RA response via the degradation of its coactivator, SRC‐3. In the case of RARγ, I demonstrated that the PRM (Proline Rich Motif) of the NTD interacts directly with one SH3 domain of Vinexin β, an adaptor protein. This association occurs only when the PRM is not phosphorylated and maintains the receptor outside of the chromatin. After RA addition, one of the serine of the PRM becomes phosphorylated, inducing the dissociation of Vinexin β, and finally the recruitment of phosphorylated RARγ to RA target‐genes. In this context, I also realized a “genome wide” bioinformatic search for finding new functional RAREs
Kammerer, Sabrina Myriam. "Etude structurale de l'interaction récepteurs nucléaires/corégulateurs et du domaine de liaison au ligand du récepteur à l'acide rétinoïque". Université Louis Pasteur (Strasbourg) (1971-2008), 2004. http://www.theses.fr/2004STR13206.
Pełny tekst źródłaNuclear receptors (NR) are ligand dependant transcription factors which share a common modular organization. The A/B domain bears the autonomous activation fonction AF1. The C domain is the DNA binding domain (DBD). The D domain contitutes a hinge between the C- and E domain. The E domain is the ligand binding domain (LBD) which also bears the ligand-dependant activation fonction AF2. NR plays an important role in the regulation of cell proliferation, differentiation, apoptosis and in cell homeostasis maintenance. Thus they are targeted by numerous treatment notably by cancer therapy, and by diabet and obesity treatments. Numerous studies uncovered the canonical three dimensional fold of LBD as well as the structural basis of agonism/antagonism. But at the begining of my PhD, the structural basis of corepresseur recruitment as well as the structural mechanism of AF1 fonction were unknown. To adress these questions we decided to undergo the two first projects of my PhD
Bruck, Nathalie. "Phosphorylation des récepteurs nucléaires de l'acide rétinoïque : Mécanisme et conséquences sur la transcription des gènes cibles". Université Louis Pasteur (Strasbourg) (1971-2008), 2008. http://www.theses.fr/2008STR13134.
Pełny tekst źródłaVernet, Nadège. "Analyse du rôle de l'acide rétinoïque et de ses récepteurs au cours de la spermatogenèse". Université Louis Pasteur (Strasbourg) (1971-2008), 2006. https://publication-theses.unistra.fr/public/theses_doctorat/2006/VERNET_Nadege_2006.pdf.
Pełny tekst źródłaIt has been known for more than a decade that retinoic acid (RA) is indispensable for the differentiation of spermatogonia, the stem cells of the spermatogenic lineage. RA acts though binding to nuclear receptors, the RAR and the RXR, which in the mouse testis have very distinct expression patterns. In particular, we detected RARg only in spermatogonia while RARa is present only in Sertoli cells, the somatic cells supporting the gem cell lineage. Selective inactivation of RARa in Sertoli cells (RaraSer-/- mutation) results in a testicular degeneration through germ cell desquamation and apoptosis. Sertoli cells lacking RARa are morphologically normal. However, they fail to express genes involved in cell adhesion (Lgals1) and loose the property to cyclically express genes encoding transcription factors (Gata1, Androgen receptor gene), membrane and secreted proteins (e. G. , Stra6). These data indicate at the very least that Rara expression in Sertoli cells is instrumental to the maintenance of the seminiferous epithelium. On the other hand, we showed that RaraSer-/- mutant mice do not recapitulate the arrest of spermatogonia maturation which we described in a situation of vitamin A-deficiency (VAD). The reasons of the differences between the VAD-induced testicular degeneration and those caused by Rara ablation are still unknown. Moreover, we revealed that, in Sertoli cells, RARa will act in RXRb-heterodimer to control spermiation and that RARa also exerts functions (Sertoli cell cycle, seminiferous epithelium integrity) independently of RXRs
Rachez, Christophe. "Détermiants structuraux du récepteurs humain alpha de l'acide rétinoïque (RAR) impliqués dans la dimérisation et la liaisin à l'ADN". Lille 1, 1996. https://pepite-depot.univ-lille.fr/LIBRE/Th_Num/1996/50376-1996-89.pdf.
Pełny tekst źródłaCoustaut, Maryse. "Expression des récepteurs nucléaires de l'acide rétinoïque et de la triiodothyronine au cours du vieillissement et d'une alcoolisation chronique". Bordeaux 1, 1996. http://www.theses.fr/1996BOR10588.
Pełny tekst źródłaPiskunov, Aleksandr. "Le récepteur nucléaire de l'acide rétinoïque alpha (RARa) : nouveaux effets non-génomiques et nouveaux partenaires". Phd thesis, Université de Strasbourg, 2012. http://tel.archives-ouvertes.fr/tel-00756292.
Pełny tekst źródłaFerry, Christine. "Activité protéolytique et non protéolytique du protéasome et de ses sous-complexes dans la réponse à l’acide rétinoïque". Strasbourg, 2010. http://www.theses.fr/2010STRA6220.
Pełny tekst źródłaThe effects of Retinoids (active derivatives of Vitamin A) are mediated by two classes of nuclear receptors, RAR (α, β, γ) and RXR (α, β, γ), which function as ligand‐dependent transcription regulators. The team demonstrated that the transcriptional activity of RARα is regulated by phosphorylation processes and by the dynamic recruitment of coregulators like SRC‐3 and of proteasomal subunits such as SUG‐1. Moreover, RARα and its coactivator SRC‐3 are degraded by the proteasome at the end of the retinoid signal. I participated to the study of non‐genomic effects of RA, initiated by kinase cascades leading to RARα phosphorylation at two serine residues (S369 and S77) and to RARα recruitment to the promoters of target genes. Then I investigated how phosphorylation and the proteasome regulate SRC‐3 activity. I have shown that SRC‐3 is recruited concomitantly with SUG‐1 to RARα target promoters and that both of them participate to the dynamics of transcription. Then, I have shown that SRC3 is phosphorylated, ubiquitinated and degraded by the proteasome. The phosphorylated residue has been identified as Serine 860. By using a siRNA hightroughput screen I identified Cullin 3 and Rbx1 as components of the E3 ligase involved in the ubiquitination/degradation of SRC‐3. In addition SRC‐3 ubiquitination depends on S860 phosphorylation and occurs out of chromatin subsequently to SRC‐3 dissociation from RARα. Finally, the proteasomal degradation of SRC‐3 also involves SUG‐1. Concerning RARα, it appears that its degradation is more complex and does not involve the classical models. Nevertheless, S369 phosphorylation and the coactivators binding surface appears to be involved. In conclusion, I highlighted a global role of the proteasome in the RA response as it is implicated in the initiation of target genes transcription as well as in the degradation of RARα and SRC‐3