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16 results on '"Roccuzzo, Michela"'

3. CD81-guided heterologous EVs present heterogeneous interactions with breast cancer cells

Author

Gurrieri, Elena, primary, Carradori, Giulia, additional, Roccuzzo, Michela, additional, Pancher, Michael, additional, Peroni, Daniele, additional, Belli, Romina, additional, Trevisan, Caterina, additional, Notarangelo, Michela, additional, Huang, Wen-Qiu, additional, Carreira, Agata SA, additional, Quattrone, Alessandro, additional, Jenster, Guido, additional, Ten Hagen, Timo L.M., additional, and D’Agostino, Vito Giuseppe, additional

Published
2024
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6. A11 Huntingtin-mediated axonal transport requires arginine methylation by PRMT6

Author

Migazzi, Alice, primary, Scaramuzzino, Chiara, additional, Anderson, Eric, additional, Tripathy, Debasmita, additional, Hernández, Ivó H, additional, Grant, Rogan, additional, Roccuzzo, Michela, additional, Tosatto, Laura, additional, Virlogeux, Amandine, additional, Zuccato, Chiara, additional, Caricasole, Andrea, additional, Ratovitski, Tamara, additional, Ross, Christopher A, additional, Pandey, Udai, additional, Lucas, José J, additional, Saudou, Frédéric, additional, Pennuto, Maria, additional, and Basso, Manuela, additional

Published
2021
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7. Huntingtin-mediated axonal transport requires arginine methylation by PRMT6

Author

Telethon Italia, Association Française contre les Myopathies, National Institutes of Health (US), Fondazione Italiana per la Ricerca sul Cancro, Associazione Alzheimer Trento, Agence Nationale de la Recherche (France), Ministerio de Ciencia, Innovación y Universidades (España), Migazzi, Alice, Scaramuzzino, Chiara, Anderson, Eric N., Tripathy, Debasmita, Hernández, Ivó H., Grant, Rogan, A, Roccuzzo, Michela, Tosatto, Laura, Virlogeux, Amandine, Zuccato, Chiara, Caricasole, Andrea, Ratovitski, Tamara, Pandey, Udai B., Lucas, José Javier, Saudou, Fréderic, Pennuto, María, Basso, Manuela, Telethon Italia, Association Française contre les Myopathies, National Institutes of Health (US), Fondazione Italiana per la Ricerca sul Cancro, Associazione Alzheimer Trento, Agence Nationale de la Recherche (France), Ministerio de Ciencia, Innovación y Universidades (España), Migazzi, Alice, Scaramuzzino, Chiara, Anderson, Eric N., Tripathy, Debasmita, Hernández, Ivó H., Grant, Rogan, A, Roccuzzo, Michela, Tosatto, Laura, Virlogeux, Amandine, Zuccato, Chiara, Caricasole, Andrea, Ratovitski, Tamara, Pandey, Udai B., Lucas, José Javier, Saudou, Fréderic, Pennuto, María, and Basso, Manuela

Abstract

The huntingtin (HTT) protein transports various organelles, including vesicles containing neurotrophic factors, from embryonic development throughout life. To better understand how HTT mediates axonal transport and why this function is disrupted in Huntington's disease (HD), we study vesicle-associated HTT and find that it is dimethylated at a highly conserved arginine residue (R118) by the protein arginine methyltransferase 6 (PRMT6). Without R118 methylation, HTT associates less with vesicles, anterograde trafficking is diminished, and neuronal death ensues—very similar to what occurs in HD. Inhibiting PRMT6 in HD cells and neurons exacerbates mutant HTT (mHTT) toxicity and impairs axonal trafficking, whereas overexpressing PRMT6 restores axonal transport and neuronal viability, except in the presence of a methylation-defective variant of mHTT. In HD flies, overexpressing PRMT6 rescues axonal defects and eclosion. Arginine methylation thus regulates HTT-mediated vesicular transport along the axon, and increasing HTT methylation could be of therapeutic interest for HD.

Published
2021

8. Huntingtin-mediated axonal transport requires arginine methylation by PRMT6

Author

Migazzi, Alice, primary, Scaramuzzino, Chiara, additional, Anderson, Eric N., additional, Tripathy, Debasmita, additional, Hernández, Ivó H., additional, Grant, Rogan A., additional, Roccuzzo, Michela, additional, Tosatto, Laura, additional, Virlogeux, Amandine, additional, Zuccato, Chiara, additional, Caricasole, Andrea, additional, Ratovitski, Tamara, additional, Ross, Christopher A., additional, Pandey, Udai B., additional, Lucas, José J., additional, Saudou, Frédéric, additional, Pennuto, Maria, additional, and Basso, Manuela, additional

Published
2021
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9. Centriolar distal appendages activate the centrosome‐PIDDosome‐p53 signalling axis via ANKRD26

Author

Burigotto, Matteo, primary, Mattivi, Alessia, additional, Migliorati, Daniele, additional, Magnani, Giovanni, additional, Valentini, Chiara, additional, Roccuzzo, Michela, additional, Offterdinger, Martin, additional, Pizzato, Massimo, additional, Schmidt, Alexander, additional, Villunger, Andreas, additional, Maffini, Stefano, additional, and Fava, Luca L, additional

Published
2020
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11. Axonal precursor mi RNA s hitchhike on endosomes and locally regulate the development of neural circuits

Author

Corradi, Eloina, primary, Dalla Costa, Irene, additional, Gavoci, Antoneta, additional, Iyer, Archana, additional, Roccuzzo, Michela, additional, Otto, Tegan A, additional, Oliani, Eleonora, additional, Bridi, Simone, additional, Strohbuecker, Stephanie, additional, Santos‐Rodriguez, Gabriela, additional, Valdembri, Donatella, additional, Serini, Guido, additional, Abreu‐Goodger, Cei, additional, and Baudet, Marie‐Laure, additional

Published
2020
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12. Vertically-Aligned Functionalized Silicon Micropillars for 3D Culture of Human Pluripotent Stem Cell-Derived Cortical Progenitors

Author

Cutarelli, Alessandro, primary, Ghio, Simone, additional, Zasso, Jacopo, additional, Speccher, Alessandra, additional, Scarduelli, Giorgina, additional, Roccuzzo, Michela, additional, Crivellari, Michele, additional, Maria Pugno, Nicola, additional, Casarosa, Simona, additional, Boscardin, Maurizio, additional, and Conti, Luciano, additional

Published
2019
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13. Vertically-Aligned Functionalized Silicon Micropillars for 3D Culture of Human Pluripotent Stem Cell-Derived Cortical Progenitors.

Author

Cutarelli, Alessandro, Ghio, Simone, Zasso, Jacopo, Speccher, Alessandra, Scarduelli, Giorgina, Roccuzzo, Michela, Crivellari, Michele, Pugno, Nicola Maria, Casarosa, Simona, Boscardin, Maurizio, and Conti, Luciano

Subjects
CEREBRAL cortex, SILICON, HUMAN embryology, TISSUE engineering, MORPHOLOGY, NEUROGLIA
Abstract

Silicon is a promising material for tissue engineering since it allows to produce micropatterned scaffolding structures resembling biological tissues. Using specific fabrication methods, it is possible to build aligned 3D network-like structures. In the present study, we exploited vertically-aligned silicon micropillar arrays as culture systems for human iPSC-derived cortical progenitors. In particular, our aim was to mimic the radially-oriented cortical radial glia fibres that during embryonic development play key roles in controlling the expansion, radial migration and differentiation of cortical progenitors, which are, in turn, pivotal to the establishment of the correct multilayered cerebral cortex structure. Here we show that silicon vertical micropillar arrays efficiently promote expansion and stemness preservation of human cortical progenitors when compared to standard monolayer growth conditions. Furthermore, the vertically-oriented micropillars allow the radial migration distinctive of cortical progenitors in vivo. These results indicate that vertical silicon micropillar arrays can offer an optimal system for human cortical progenitors’ growth and migration. Furthermore, similar structures present an attractive platform for cortical tissue engineering. [ABSTRACT FROM AUTHOR]

Published
2020
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14. miR-182 Regulates Slit2-Mediated Axon Guidance by Modulating the Local Translation of a Specific mRNA

Author

Bellon, Anaïs, primary, Iyer, Archana, additional, Bridi, Simone, additional, Lee, Flora C.Y., additional, Ovando-Vázquez, Cesaré, additional, Corradi, Eloina, additional, Longhi, Sara, additional, Roccuzzo, Michela, additional, Strohbuecker, Stephanie, additional, Naik, Sindhu, additional, Sarkies, Peter, additional, Miska, Eric, additional, Abreu-Goodger, Cei, additional, Holt, Christine E., additional, and Baudet, Marie-Laure, additional

Published
2017
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15. REGULATION OF CHROMOSOME SEGREGATION BY CONSERVED PHOSPHATASE CDC14 AND KINASE CDC5

Author

ROCCUZZO, MICHELA

Abstract

The faithful transmission of the replicated genome from the mother to the daughter cell requires the correct establishment of linkages between the duplicated chromosomes (sister chromatids) and their bi-orientation on the mitotic spindle. Chromosome segregation initiates only after each sisters pair is correctly aligned onto the microtubules emanating from the spindle poles. Next, Esp1-mediated cleavage of cohesin is required to trigger anaphase onset while the physical segregation of the separated sisters is next driven by spindle activity. However, this scenario appears to be more complicated involving additional factors driving the sister chromatid segregation process (i.e. the Top2-mediated resolution of replication catenates). In budding yeast, anaphase progression and exit from mitosis require the protein phosphatase Cdc14 whose activation relies on two consecutive protein pathways, the FEAR network and the MEN. As the polo-like kinase Cdc5 is a component of both pathways its activity is essential to Cdc14 release and in its absence Cdc14 is never released. By combining loss-of-function alleles of Cdc5 and Cdc14 we obtained double mutant cells that had cohesin cleaved but still arrested with undivided nuclei and short bipolar spindles. Anaphase spindle elongation initiates quickly after cohesin removal (anaphase A) and then switches to a slower elongation rate (anaphase B) due to changes in spindle behaviour mediated by motor proteins and microtubule-associated enzymes. Although some residual cohesion between sister chromatids seems to contribute to the terminal phenotype of cdc14 cdc5 cells, our data indicate that anaphase B is the main mitotic defect of these cells. We conclude that Cdc5 and Cdc14 are redundantly involved in activating spindle activity following cohesion resolution, suggesting the existence of a regulatory network that coordinates sister chromatid separation with spindle elongation after cohesin cleavage. Importantly, we identified the motor protein Cin8 as a (direct or indirect) target of Cdc5 in the regulation of spindle elongation.

Published
2014
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