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15 results on '"Verrico, Annalisa"'

2. New 6- and 7-heterocyclyl-1H-indole derivatives as potent tubulin assembly and cancer cell growth inhibitors

Author

La Regina, Giuseppe, Bai, Ruoli, Coluccia, Antonio, Naccarato, Valentina, Famiglini, Valeria, Nalli, Marianna, Masci, Domiziana, Verrico, Annalisa, Rovella, Paola, Mazzoccoli, Carmela, Da Pozzo, Eleonora, Cavallini, Chiara, Martini, Claudia, Vultaggio, Stefania, Dondio, Giulio, Varasi, Mario, Mercurio, Ciro, Hamel, Ernest, Lavia, Patrizia, and Silvestri, Romano

Published
2018
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12. New Indole Tubulin Assembly Inhibitors Cause Stable Arrest of Mitotic Progression, Enhanced Stimulation of Natural Killer Cell Cytotoxic Activity, and Repression of Hedgehog-Dependent Cancer

Author

La Regina, Giuseppe, primary, Bai, Ruoli, additional, Coluccia, Antonio, additional, Famiglini, Valeria, additional, Pelliccia, Sveva, additional, Passacantilli, Sara, additional, Mazzoccoli, Carmela, additional, Ruggieri, Vitalba, additional, Verrico, Annalisa, additional, Miele, Andrea, additional, Monti, Ludovica, additional, Nalli, Marianna, additional, Alfonsi, Romina, additional, Di Marcotullio, Lucia, additional, Gulino, Alberto, additional, Ricci, Biancamaria, additional, Soriani, Alessandra, additional, Santoni, Angela, additional, Caraglia, Michele, additional, Porto, Stefania, additional, Da Pozzo, Eleonora, additional, Martini, Claudia, additional, Brancale, Andrea, additional, Marinelli, Luciana, additional, Novellino, Ettore, additional, Vultaggio, Stefania, additional, Varasi, Mario, additional, Mercurio, Ciro, additional, Bigogno, Chiara, additional, Dondio, Giulio, additional, Hamel, Ernest, additional, Lavia, Patrizia, additional, and Silvestri, Romano, additional

Published
2015
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13. Importin-ß and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function.

Author

Gilistro, Eugenia, de Turris, Valeria, Damizia, Michela, Verrico, Annalisa, Moroni, Sara, De Santis, Riccardo, Rosa, Alessandro, and Lavia, Patrizia

Subjects
SMALL ubiquitin-related modifier proteins, PROTEINS, NUCLEOPORINS, GUANOSINE triphosphatase, MITOSIS, NUCLEAR transport (Cytology), DNA topoisomerase II
Abstract

Protein conjugation with small ubiquitin-related modifier (SUMO) is a post-translational modification that modulates protein interactions and localisation. RANBP2 is a large nucleoporin endowed with SUMO E3 ligase and SUMO-stabilising activity, and is implicated in some cancer types. RANBP2 is part of a larger complex, consisting of SUMO-modified RANGAP1, the GTP-hydrolysis activating factor for the GTPase RAN. During mitosis, the RANBP2-SUMO-RANGAP1 complex localises to the mitotic spindle and to kinetochores after microtubule attachment. Here, we address the mechanisms that regulate this localisation and how they affect kinetochore functions. Using proximity ligation assays, we find that nuclear transport receptors importin-ß and CRM1 play essential roles in localising the RANBP2-SUMO-RANGAP1 complex away from, or at kinetochores, respectively. Using newly generated inducible cell lines, we show that overexpression of nuclear transport receptors affects the timing of RANBP2 localisation in opposite ways. Concomitantly, kinetochore functions are also affected, including the accumulation of SUMO-conjugated topoisomerase-IIa and stability of kinetochore fibres. These results delineate a novel mechanism through which nuclear transport receptors govern the functional state of kinetochores by regulating the timely deposition of RANBP2. [ABSTRACT FROM AUTHOR]

Published
2017
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14. New indole tubulin assembly inhibitors cause stable arrest of mitotic progression, enhanced stimulation of natural killer cell cytotoxic activity, and repression of hedgehog-dependent cancer

Author

Eleonora Da Pozzo, Stefania Vultaggio, Andrea Miele, Valeria Famiglini, Vitalba Ruggieri, Claudia Martini, Antonio Coluccia, Ettore Novellino, Sveva Pelliccia, Michele Caraglia, Ruoli Bai, Alberto Gulino, Chiara Bigogno, Biancamaria Ricci, Sara Passacantilli, Alessandra Soriani, Marianna Nalli, Luciana Marinelli, Ciro Mercurio, Giuseppe La Regina, Ludovica Monti, Angela Santoni, Giulio Dondio, Ernest Hamel, Andrea Brancale, Romina Alfonsi, Mario Varasi, Patrizia Lavia, Carmela Mazzoccoli, Lucia Di Marcotullio, Annalisa Verrico, Stefania Porto, Romano Silvestri, La Regina, Giuseppe, Bai, Ruoli, Coluccia, Antonio, Famiglini, Valeria, Pelliccia, Sveva, Passacantilli, Sara, Mazzoccoli, Carmela, Ruggieri, Vitalba, Verrico, Annalisa, Miele, Andrea, Monti, Ludovica, Nalli, Marianna, Alfonsi, Romina, Di Marcotullio, Lucia, Gulino, Alberto, Ricci, Biancamaria, Soriani, Alessandra, Santoni, Angela, Caraglia, Michele, Porto, Stefania, Da Pozzo, Eleonora, Martini, Claudia, Brancale, Andrea, Marinelli, Luciana, Novellino, Ettore, Vultaggio, Stefania, Varasi, Mario, Mercurio, Ciro, Bigogno, Chiara, Dondio, Giulio, Hamel, Ernest, Lavia, Patrizia, and Silvestri, Romano

Subjects
Cytotoxicity, Immunologic, Indoles, Cell cycle checkpoint, HeLa, Mice, Tubulin, Neoplasms, Drug Discovery, Cytotoxic T cell, 2-phenylindole, tubulin, tubulin polymerization, NIH 3T3 Cell, Cancer, biology, Chemistry, Medicine (all), Cell cycle, Mitosi, Hedgehog signaling pathway, Cell biology, Killer Cells, Natural, tubulin polymerization, medicine.anatomical_structure, mitotic progression, Hedgehog signaling activation, tubulin polymerization, cancer cell growth, Molecular Medicine, Hedgehog Protein, Cell Division, Human, RM, Mitosis, cancer cell growth, Article, Natural killer cell, RC0254, Cell Line, Tumor, medicine, Animals, Humans, Hedgehog Proteins, Hedgehog signaling activation, Animal, Drug Discovery3003 Pharmaceutical Science, Tubulin inhbitors, mitotic progression, biology.organism_classification, Cell culture, Drug Resistance, Neoplasm, Indole, Cancer cell, NIH 3T3 Cells, Neoplasm, Hedgehog
Abstract

We designed 39 new 2-phenylindole derivatives as potential anticancer agents bearing the 3,4,5-trimethoxyphenyl moiety with a sulfur, ketone, or methylene bridging group at position 3 of the indole and with halogen or methoxy substituent(s) at positions 4-7. Compounds 33 and 44 strongly inhibited the growth of the P-glycoprotein-overexpressing multi-drug-resistant cell lines NCI/ADR-RES and Messa/Dx5. At 10 nM, 33 and 44 stimulated the cytotoxic activity of NK cells. At 20-50 nM, 33 and 44 arrested >80% of HeLa cells in the G2/M phase of the cell cycle, with stable arrest of mitotic progression. Cell cycle arrest was followed by cell death. Indoles 33, 44, and 81 showed strong inhibition of the SAG-induced Hedgehog signaling activation in NIH3T3 Shh-Light II cells with IC50 values of 19, 72, and 38 nM, respectively. Compounds of this class potently inhibited tubulin polymerization and cancer cell growth, including stimulation of natural killer cell cytotoxic activity and repression of Hedgehog-dependent cancer.

Published
2015

15. Visualization of human karyopherin beta-1/importin beta-1 interactions with protein partners in mitotic cells by co-immunoprecipitation and proximity ligation assays

Author

Laura Di Francesco, Annalisa Verrico, Patrizia Lavia, Giulia Guarguaglini, Maria Eugenia Schininà, Italia Anna Asteriti, Paola Rovella, and Pietro Cirigliano

Subjects
0301 basic medicine, import receptor kpn-beta-1, chromosome alignment, nuclear transporter, mammalian-cells, rangtp gradient, messenger-rna, spindle poles, up-regulation, mitosis, cancer, Interactome, Mitosis, lcsh:Medicine, Importin, Proximity ligation assay, Biology, Polymerase Chain Reaction, environment and public health, Article, 03 medical and health sciences, Nuclear transport receptors, Image Processing, Computer-Assisted, Humans, Immunoprecipitation, Protein interaction networks, Protein Interaction Domains and Motifs, lcsh:Science, Karyopherin, chemistry.chemical_classification, Multidisciplinary, lcsh:R, Cell cycle, beta Karyopherins, Cell biology, 030104 developmental biology, chemistry, Ran, embryonic structures, Biological Assay, Beta Karyopherins, lcsh:Q, Nuclear transport, HeLa Cells
Abstract

Karyopherin beta-1/Importin beta-1 is a conserved nuclear transport receptor, acting in protein nuclear import in interphase and as a global regulator of mitosis. These pleiotropic functions reflect its ability to interact with, and regulate, different pathways during the cell cycle, operating as a major effector of the GTPase RAN. Importin beta-1 is overexpressed in cancers characterized by high genetic instability, an observation that highlights the importance of identifying its partners in mitosis. Here we present the first comprehensive profile of importin beta-1 interactors from human mitotic cells. By combining co-immunoprecipitation and proteome-wide mass spectrometry analysis of synchronized cell extracts, we identified expected (e.g., RAN and SUMO pathway factors) and novel mitotic interactors of importin beta-1, many with RNA-binding ability, that had not been previously associated with importin beta-1. These data complement interactomic studies of interphase transport pathways. We further developed automated proximity ligation assay (PLA) protocols to validate selected interactors. We succeeded in obtaining spatial and temporal resolution of genuine importin beta-1 interactions, which were visualized and localized in situ in intact mitotic cells. Further developments of PLA protocols will be helpful to dissect importin beta-1-orchestrated pathways during mitosis.

Published
2018

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