Sara Moroni
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Sara Moroni has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
- Andrea Musacchio
Max Planck Institute of Molecular Physiology
1 shared publication - Carolin Koerner
Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
1 shared publication - Erica Di Cesare
Institute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185 Rome, Italy
1 shared publication - Jessica Bartoli
Institute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185 Rome, Italy
1 shared publication - Maria Giubettini
CrestOptics S.p.a. , Rome
1 shared publication - Michela Damizia
Institute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185 Rome, Italy
1 shared publication
Latest Publications
- Open Access
Aurora B SUMOylation Is Restricted to Centromeres in Early Mitosis and Requires RANBP2
Conjugation with the small ubiquitin-like modifier (SUMO) modulates protein interactions and localisation. The kinase Aurora B, a key regulator of mitosis, was previously identified as a SUMOylation target in vitro and in assays with overexpressed components. However, where and when this modification genuinely occurs in human cells was not ascertained. Here, we have developed intramolecular Proximity Ligation Assays (PLA) to visualise SUMO-conjugated Aurora B in human cells in situ. We visualised Aurora B-SUMO products at centromeres in prometaphase and metaphase, which declined from anaphase onwards and became virtually undetectable at cytokinesis. In the mitotic window in which Aurora B/SUMO products are abundant, Aurora B co-localised and interacted with NUP358/RANBP2, a nucleoporin with SUMO ligase and SUMO-stabilising activity. Indeed, in addition to the requirement for the previously identified PIAS3 SUMO ligase, we found that NUP358/RANBP2 is also implicated in Aurora B-SUMO PLA product formation and centromere localisation. In summary, SUMOylation marks a distinctive window of Aurora B functions at centromeres in prometaphase and metaphase while being dispensable for functions exerted in cytokinesis, and RANBP2 contributes to this control, adding a novel layer to modulation of Aurora B functions during mitosis.
Open AccessAurora B SUMOylation Is Restricted to Centromeres in Early Mitosis and Requires RANBP2
Conjugation with the small ubiquitin-like modifier (SUMO) modulates protein interactions and localisation. The kinase Aurora B, a key regulator of mitosis, was previously identified as a SUMOylation target in vitro and in assays with overexpressed components. However, where and when this modification genuinely occurs in human cells was not ascertained. Here, we have developed intramolecular Proximity Ligation Assays (PLA) to visualise SUMO-conjugated Aurora B in human cells in situ. We visualised Aurora B-SUMO products at centromeres in prometaphase and metaphase, which declined from anaphase onwards and became virtually undetectable at cytokinesis. In the mitotic window in which Aurora B/SUMO products are abundant, Aurora B co-localised and interacted with NUP358/RANBP2, a nucleoporin with SUMO ligase and SUMO-stabilising activity. Indeed, in addition to the requirement for the previously identified PIAS3 SUMO ligase, we found that NUP358/RANBP2 is also implicated in Aurora B-SUMO PLA product formation and centromere localisation. In summary, SUMOylation marks a distinctive window of Aurora B functions at centromeres in prometaphase and metaphase while being dispensable for functions exerted in cytokinesis, and RANBP2 contributes to this control, adding a novel layer to modulation of Aurora B functions during mitosis.