Letteratura scientifica selezionata sul tema "Complexe adapteur AP-1"
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Articoli di riviste sul tema "Complexe adapteur AP-1":
Yeung, Bonny G., Huan L. Phan e Gregory S. Payne. "Adaptor Complex-independent Clathrin Function in Yeast". Molecular Biology of the Cell 10, n. 11 (novembre 1999): 3643–59. http://dx.doi.org/10.1091/mbc.10.11.3643.
Salazar, G., B. Craige, M. L. Styers, K. A. Newell-Litwa, M. M. Doucette, B. H. Wainer, J. M. Falcon-Perez et al. "BLOC-1 Complex Deficiency Alters the Targeting of Adaptor Protein Complex-3 Cargoes". Molecular Biology of the Cell 17, n. 9 (settembre 2006): 4014–26. http://dx.doi.org/10.1091/mbc.e06-02-0103.
Fölsch, Heike, Marc Pypaert, Sandra Maday, Laurence Pelletier e Ira Mellman. "The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains". Journal of Cell Biology 163, n. 2 (27 ottobre 2003): 351–62. http://dx.doi.org/10.1083/jcb.200309020.
Kim, Myung-Hee, e Louis B. Hersh. "The Vesicular Acetylcholine Transporter Interacts with Clathrin-associated Adaptor Complexes AP-1 and AP-2". Journal of Biological Chemistry 279, n. 13 (14 gennaio 2004): 12580–87. http://dx.doi.org/10.1074/jbc.m310681200.
Sorkina, T., A. Bild, F. Tebar e A. Sorkin. "Clathrin, adaptors and eps15 in endosomes containing activated epidermal growth factor receptors". Journal of Cell Science 112, n. 3 (1 febbraio 1999): 317–27. http://dx.doi.org/10.1242/jcs.112.3.317.
Fölsch, Heike, Marc Pypaert, Peter Schu e Ira Mellman. "Distribution and Function of Ap-1 Clathrin Adaptor Complexes in Polarized Epithelial Cells". Journal of Cell Biology 152, n. 3 (5 febbraio 2001): 595–606. http://dx.doi.org/10.1083/jcb.152.3.595.
BAROIS, Nicolas, e Oddmund BAKKE. "The adaptor protein AP-4 as a component of the clathrin coat machinery: a morphological study". Biochemical Journal 385, n. 2 (7 gennaio 2005): 503–10. http://dx.doi.org/10.1042/bj20041010.
Lefkir, Yaya, Benoît de Chassey, Annick Dubois, Aleksandra Bogdanovic, Rebecca J. Brady, Olivier Destaing, Franz Bruckert, Theresa J. O'Halloran, Pierre Cosson e François Letourneur. "The AP-1 Clathrin-adaptor Is Required for Lysosomal Enzymes Sorting and Biogenesis of the Contractile Vacuole Complex in Dictyostelium Cells". Molecular Biology of the Cell 14, n. 5 (maggio 2003): 1835–51. http://dx.doi.org/10.1091/mbc.e02-10-0627.
Nie, Z. "The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3". Journal of Cell Science 118, n. 15 (1 agosto 2005): 3555–66. http://dx.doi.org/10.1242/jcs.02486.
LUNDMARK, Richard, e Sven R. CARLSSON. "The β-appendages of the four adaptor-protein (AP) complexes: structure and binding properties, and identification of sorting nexin 9 as an accessory protein to AP-2". Biochemical Journal 362, n. 3 (8 marzo 2002): 597–607. http://dx.doi.org/10.1042/bj3620597.
Tesi sul tema "Complexe adapteur AP-1":
Ferrié, Martin. "Étude de la maturation protéolytique et du trafic intracellulaire de la protéine de capside ORF2 du virus de l'hépatite E (HEV)". Electronic Thesis or Diss., Université de Lille (2022-....), 2023. http://www.theses.fr/2023ULILS067.
Hepatitis E virus (HEV) infection is a major public health problem, affecting an estimated 100 million people and killing 100,000 every year worldwide. HEV is the leading cause of acute hepatitis worldwide. In France, seroprevalence is 22.4%. This virus is transmitted via the feco-oral route, or by eating contaminated undercooked meat. During my thesis, I focused on the ORF2 capsid protein, which is the structural unit of viral particles and a central player in the HEV lifecycle. ORF2 is a 660 amino acid protein with an N-terminal signal peptide and three potential N-glycosylation sites. During its lifecycle, HEV produces at least three forms of its capsid protein: (i) the ORF2g (for glycosylated) form and (ii) the ORF2c (for cleaved) form, abbreviated ORF2g/c, which are glycosylated forms and massively secreted in culture supernatants or serum from infected patients, and (iii) the ORF2i (for infectious) form, which is not glycosylated and is associated with viral particles.As part of my thesis work, I studied the mechanisms of proteolytic maturation and intracellular trafficking of the ORF2 protein. More specifically, I first showed that ORF2 is imported into the nucleus of infected cells via an Importin-alpha1-dependent mechanism, thanks to an arginine-rich motif located at the N-terminus of ORF2 and named ARM. The ORF2 protein is then exported to the cytoplasm via a CRM1 exportin-dependent mechanism, thanks to three nuclear export sites (NES9, NES10 and NES12) that we have identified in the ORF2 sequence. I have also shown that nucleocytoplasmic trafficking of ORF2 probably regulates the expression of certain antiviral immunity genes in the early stages of infection.Secondly, I participated in the identification and characterization of HEV viral factories. We have shown that the viral proteins ORF1, ORF2 and ORF3, as well as viral RNA, are enriched in vesicular and tubular structures located in the perinuclear regions of infected cells. We have shown that these structures are also enriched in markers of the endosomal recycling compartment (ERC), such as Rab11 and CD71, indicating that HEV viral factories probably derive from the ERC. By performing Rab11 silencing experiments with siRNAs, we confirmed the importance of the ERC in the production of HEV viral particles. Thirdly, I demonstrated that the ORF2i protein, which is associated with the membranes of the secretion pathway, is addressed to viral factories by a mechanism involving the AP-1 adaptor complex.In a fourth step, I characterized the proteolytic maturation mechanisms of the ORF2g/c and ORF2i forms. I showed that furin, a proproprotein convertase of the secretory pathway, is involved in the proteolytic maturation of ORF2g/c glycoproteins. I have also shown that presenilin, which is the catalytic subunit of the macro-complex Gamma-secretase, is involved in the proteolytic maturation of the ORF2i form. Interestingly, I have shown that pharmacological inhibition of presenilin drastically reduces viral infectivity in human hepatocarcinoma lines and in primary human hepatocytes. These data suggest that pharmacological inhibition of presenilin represents a promising antiviral strategy. In conclusion, the results obtained during my thesis provide a better understanding of the mechanisms of subcellular addressing and proteolytic maturation of the ORF2 capsid protein, and pave the way for the development of new therapies to combat HEV
Dugast, Marc. "Mécanismes de tri impliqués dans le trafic intracellulaire des molécules du CMH II et dans les effets de Nef du VIH-1 sur les CMH et CD4". Paris 7, 2005. http://www.theses.fr/2005PA077016.
Shafaq-Zadah, Massiullah. "Rôle du complexe adaptateur pour la clathrine AP-1 dans le maintien de la polarité épithéliale chez Caenorhabditis elegans". Phd thesis, Université Rennes 1, 2012. http://tel.archives-ouvertes.fr/tel-00683716.
Foote, Christopher. "The role of the AP-1 adaptor complex in trafficking between the trans-Golgi Network and endosomal system". Diss., Columbia, Mo. : University of Missouri-Columbia, 2005. http://hdl.handle.net/10355/4172.
The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from title screen of research.pdf file viewed on (November 7, 2006) Vita. Includes bibliographical references.
Duvoix, Annelyse. "Régulation transcriptionnelle de la glutathion S-transférase P1-1 via AP-1 et NF-kB dans les cellules leucémiques humaines@ : effet inhibiteur des agents chimiopréventifs d'origine naturelle". Nancy 1, 2003. http://docnum.univ-lorraine.fr/public/SCD_T_2003_0248_DUVOIX.pdf.
Rahmani, Mohamed. "Etude du complexe AP-1 dans les hépatocytes de rat traités par les facteurs de croissance et les promoteurs tumoraux : activation, composition et coopération avec NF-kB". Paris 7, 1999. http://www.theses.fr/1999PA077211.
Tavares, Lucas Alves. "O envolvimento da proteína adaptadora 1 (AP-1) no mecanismo de regulação negativa do receptor CD4 por Nef de HIV-1". Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/17/17136/tde-06012017-113215/.
The Human Immunodeficiency Virus (HIV) is the etiologic agent of Acquired Immunodeficiency Syndrome (AIDS). AIDS is a disease which has a global distribution, and it is estimated that there are currently at least 36.9 million people infected with the virus. During the replication cycle, HIV promotes several changes in the physiology of the host cell to promote their survival and enhance replication. The fast progression of HIV-1 in humans and animal models is closely linked to the function of an accessory protein Nef. Among several actions of Nef, one is the most important is the down-regulation of proteins from the immune response, such as the CD4 receptor. It is known that this action causes CD4 degradation in lysosome, but the molecular mechanisms are still incompletely understood. Nef forms a tripartite complex with the cytosolic tail of the CD4 and adapter protein 2 (AP-2) in clathrin-coated vesicles, inducing CD4 internalization and lysosome degradation. Previous research has demonstrated that CD4 target to lysosomes by Nef involves targeting of this receptor to multivesicular bodies (MVBs) pathway by an atypical mechanism because, although not need charging ubiquitination, depends on the proteins from ESCRTs (Endosomal Sorting Complexes Required for Transport) machinery and the action of Alix, an accessory protein ESCRT machinery. It has been reported that Nef interacts with subunits of AP- 1, AP-2, AP-3 complexes and Nef does not appear to interact with AP-4 and AP-5 subunits. However, the role of Nef interaction with AP-1 or AP-3 in CD4 down-regulation is poorly understood. Furthermore, AP-1, AP-2 and AP-3 are potentially heterogeneous due to the existence of multiple subunits isoforms encoded by different genes. However, there are few studies to demonstrate if the different combinations of APs isoforms are form and if they have distinct functional properties. This study aim to identify and characterize cellular factors involved on CD4 down-modulation induced by Nef from HIV-1. More specifically, this study aimed to characterize the involvement of AP-1 complex in the down-regulation of CD4 by Nef HIV-1 through the functional study of the two isoforms of ?-adaptins, AP-1 subunits. By pull-down technique, we showed that Nef is able to interact with ?2. In addition, our data from immunoblots indicated that ?2- adaptin, not ?1-adaptin, is required in Nef-mediated targeting of CD4 to lysosomes and the ?2 participation in this process is conserved by Nef from different viral strains. Furthermore, by flow cytometry assay, ?2 depletion, but not ?1 depletion, compromises the reduction of surface CD4 levels induced by Nef. Immunofluorescence microscopy analysis also revealed that ?2 depletion impairs the redistribution of CD4 by Nef to juxtanuclear region, resulting in CD4 accumulation in primary endosomes. Knockdown of ?1A, another subunit of AP-1, resulted in decreased cellular levels of ?1 and ?2 and, compromising the efficient CD4 degradation by Nef. Moreover, upon artificially stabilizing ESCRT-I in early endosomes, via overexpression of HRS, internalized CD4 accumulates in enlarged HRS-GFP positive endosomes, where co-localize with ?2. Together, the results indicate that ?2-adaptin is a molecule that is essential for CD4 targeting by Nef to ESCRT/MVB pathway, being an important protein in the endo-lysosomal system. Furthermore, the results indicate that ?-adaptins isoforms not only have different functions, but also seem to compose AP-1 complex with distinct cell functions, and only the AP-1 variant comprising ?2, but not ?1, acts in the CD4 down-regulation induced by Nef. These studies contribute to a better understanding on the molecular mechanisms involved in Nef activities, which may also help to improve the understanding of the HIV pathogenesis and the related syndrome. In addition, this work contributes with the understanding of primordial process regulation on intracellular trafficking of transmembrane proteins.
Riel, Constanze. "σ1-adaptin - the Small Subunit of the Clathrin Adaptor Complex AP-1". Doctoral thesis, 2004. http://hdl.handle.net/11858/00-1735-0000-0006-ABD8-5.
Mishra, Ratnakar. "Mechanisms of synaptic plasticity mediated by Clathrin Adaptor-protein complexes 1 and 2 in mice". Doctoral thesis, 2019. http://hdl.handle.net/21.11130/00-1735-0000-0003-C12E-0.
Riel, Constanze [Verfasser]. "σ1-adaptin [sigma-1-adaptin] : the small subunit of the clathrin adaptor complex AP-1 [[Elektronische Ressource]] / vorgelegt von Constanze Riel". 2005. http://d-nb.info/976246805/34.