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Academic literature on the topic 'RanBP2 (Nup358)'
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Journal articles on the topic "RanBP2 (Nup358)"
Bernad, Rafael, Hella van der Velde, Maarten Fornerod, and Helen Pickersgill. "Nup358/RanBP2 Attaches to the Nuclear Pore Complex via Association with Nup88 and Nup214/CAN and Plays a Supporting Role in CRM1-Mediated Nuclear Protein Export." Molecular and Cellular Biology 24, no. 6 (March 15, 2004): 2373–84. http://dx.doi.org/10.1128/mcb.24.6.2373-2384.2004.
Full textShen, Qingtang, Yifan E. Wang, Mathew Truong, Kohila Mahadevan, Jingze J. Wu, Hui Zhang, Jiawei Li, Harrison W. Smith, Craig A. Smibert, and Alexander F. Palazzo. "RanBP2/Nup358 enhances miRNA activity by sumoylating Argonautes." PLOS Genetics 17, no. 2 (February 18, 2021): e1009378. http://dx.doi.org/10.1371/journal.pgen.1009378.
Full textSwaminathan, Sowmya, Florian Kiendl, Roman Körner, Raffaella Lupetti, Ludger Hengst, and Frauke Melchior. "RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly." Journal of Cell Biology 164, no. 7 (March 22, 2004): 965–71. http://dx.doi.org/10.1083/jcb.200309126.
Full textHutten, Saskia, Annette Flotho, Frauke Melchior, and Ralph H. Kehlenbach. "The Nup358-RanGAP Complex Is Required for Efficient Importin α/β-dependent Nuclear Import." Molecular Biology of the Cell 19, no. 5 (May 2008): 2300–2310. http://dx.doi.org/10.1091/mbc.e07-12-1279.
Full textPrunuske, Amy J., Jin Liu, Suzanne Elgort, Jomon Joseph, Mary Dasso, and Katharine S. Ullman. "Nuclear Envelope Breakdown Is Coordinated by Both Nup358/RanBP2 and Nup153, Two Nucleoporins with Zinc Finger Modules." Molecular Biology of the Cell 17, no. 2 (February 2006): 760–69. http://dx.doi.org/10.1091/mbc.e05-06-0485.
Full textHutten, Saskia, and Ralph H. Kehlenbach. "Nup214 Is Required for CRM1-Dependent Nuclear Protein Export In Vivo." Molecular and Cellular Biology 26, no. 18 (September 15, 2006): 6772–85. http://dx.doi.org/10.1128/mcb.00342-06.
Full textJiang, Jing, Yifan E. Wang, Alexander F. Palazzo, and Qingtang Shen. "Roles of Nucleoporin RanBP2/Nup358 in Acute Necrotizing Encephalopathy Type 1 (ANE1) and Viral Infection." International Journal of Molecular Sciences 23, no. 7 (March 24, 2022): 3548. http://dx.doi.org/10.3390/ijms23073548.
Full textDi Cesare, Erica, Sara Moroni, Jessica Bartoli, Michela Damizia, Maria Giubettini, Carolin Koerner, Veronica Krenn, Andrea Musacchio, and Patrizia Lavia. "Aurora B SUMOylation Is Restricted to Centromeres in Early Mitosis and Requires RANBP2." Cells 12, no. 3 (January 19, 2023): 372. http://dx.doi.org/10.3390/cells12030372.
Full textLi, Jiawei, Lili Su, Jing Jiang, Yifan E. Wang, Yingying Ling, Yi Qiu, Huahui Yu, et al. "RanBP2/Nup358 Mediates Sumoylation of STAT1 and Antagonizes Interferon-α-Mediated Antiviral Innate Immunity." International Journal of Molecular Sciences 25, no. 1 (December 25, 2023): 299. http://dx.doi.org/10.3390/ijms25010299.
Full textPalazzo, Alexander F., Jomon Joseph, Ming Lim, and Kiran T. Thakur. "Workshop on RanBP2/Nup358 and acute necrotizing encephalopathy." Nucleus 13, no. 1 (April 29, 2022): 154–69. http://dx.doi.org/10.1080/19491034.2022.2069071.
Full textDissertations / Theses on the topic "RanBP2 (Nup358)"
Carlón-Andrés, Irene. "Implication fonctionnelle de la nucléoporine Nup358/RanBP2 et des récepteurs de transport dans l’entrée du génome adénoviral." Thesis, Bordeaux, 2017. http://www.theses.fr/2017BORD0807/document.
Full textNuclear delivery of viral genomes is an essential step for nuclear replicating DNA viruses such asAdenovirus (AdV). AdV particles reach the nuclear pore complex (NPC) in the form of genomecontaining, partially disassembled capsids, through a poorly understood CRM1-dependent mechanism.These capsids exceed the NPC size limit and therefore, they must disassemble at the NPC to releasethe viral genome. Nuclear import of DNA cargos is not a physiological process. Consequently, AdVneed to divert the cellular transport machinery for nuclear genome delivery. The NPC is a multiproteincomplex consisting of nucleoporins (Nups). The Nup358/RanBP2 is the major component ofthe cytoplasmic filaments of the NPC and serves as binding platform for factors includingkaryopherins (i.e Importin-β, CRM1) and the small GTPase Ran. Selective transport of cargo throughthe NPC is mediated by karyopherins, which recognize specific signals within the cargos and facilitatetheir transport in a RanGTP-dependent regulated manner. We identified that Nup358-depleted cellsreduce nuclear import efficiency of the AdV genome. Indeed, we observed that karyopherins are ratelimitingfor AdV genome import under these conditions and we mapped the minimal region ofNup358 necessary to compensate the import defect. On the other hand, we could confirm therequirement of CRM1 in nuclear targeting of AdV capsids and identified and additional role inmediating AdV capsid disassembly. This work helps to understand the strategy used by AdV todeliver their genome and gives insight about how viruses hijack the cellular transport machinery fortheir own benefit
Lin, Junyan. "Assembly and function of cytosolic nuclear pore complexes." Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAJ037.
Full textNuclear pore complexes (NPCs), huge protein assemblies built into the nuclear envelope (NE), serve as pivotal structures for bidirectional transport, maintaining the equilibrium between the nucleus and cytoplasm. Beyond their residence within the NE, NPCs are also found in stacked cytoplasmic membranes known as annulate lamellae (AL). However, the function and pathways governing the biogenesis of AL remain enigmatic. Our investigation in mammalian cells unveils a mechanism wherein AL formation arises through the fusion of pre-assembled cytosolic NPCs. The movement of cytosolic NPCs is intricately linked to the dynamics of the endoplasmic reticulum (ER), as they migrate towards and integrate into NE during early interphase under normal growth conditions, a process mediated by microtubules. RanBP2 (Nup358), a constituent of the NPC cytoplasmic filaments, emerges as necessary and sufficient for AL formation in the cytoplasm. Mechanistically, the FG repeats in the N-terminus of RanBP2 play a pivotal role by orchestrating the oligomerization state of the NPC outer ring units, known as Y-complexes. Our study elucidates an assembly process crucial for NE nourishment, ensuring the functionality of nuclear pores and underscoring the significance of cytosolic NPCs in mammalian cellular homeostasis