Antonella Di Costanzo
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Antonella Di Costanzo has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
Angela Nebbioso
Department of Biochemistry, Biophysics and General Pathology, University of Campania “Luigi Vanvitelli”, Vico L. De Crecchio 7, 80138, Napoli, Italy
1 shared publication- Antimo Migliaccio
Dept of Precision Medicine, University of Campania “L.Vanvitelli”, Naples, Italy
1 shared publication - Carmela Dell’aVersana
Department of Precision Medicine, University of Campania “Luigi Vanvitelli”, Naples, Italy
1 shared publication Hugues de Thé
INSERM Unite ́ Mixte de Recherche 944, Equipe labellisée par la Ligue Nationale contre le Cancer, Institut Universitaire d’Hématologie, Hôpital St. Louis, Paris Cedex 10, France
1 shared publication- Lidio Conte
Collège de France, Oncologie Cellulaire et Moléculaire, PSL University, INSERM UMR 1050, CNRS UMR 7241, Paris, France
1 shared publication - Lucia Altucci
Department of Precision Medicine, University of Campania “Luigi Vanvitelli”, Vico L. de Crecchio 7, Naples, Italy
1 shared publication
Latest Publications
- Open Access
- 22 February 2018
- Published by Springer Nature in Oncogene
- Vol. 37 (19) , 2559-2572
The HDAC inhibitor SAHA regulates CBX2 stability via a SUMO-triggered ubiquitin-mediated pathway in leukemia
Polycomb group (PcG) proteins regulate transcription, playing a key role in stemness and differentiation. Deregulation of PcG members is known to be involved in cancer pathogenesis. Emerging evidence suggests that CBX2, a member of the PcG protein family, is overexpressed in several human tumors, correlating with lower overall survival. Unraveling the mechanisms regulating CBX2 expression may thus provide a promising new target for anticancer strategies. Here we show that the HDAC inhibitor SAHA regulates CBX2 stability via a SUMO-triggered ubiquitin-mediated pathway in leukemia. We identify CBX4 and RNF4 as the E3 SUMO and E3 ubiquitin ligase, respectively, and describe the specific molecular mechanism regulating CBX2 protein stability. Finally, we show that CBX2-depleted leukemic cells display impaired proliferation, underscoring its critical role in regulating leukemia cell tumorogenicity. Our results show that SAHA affects CBX2 stability, revealing a potential SAHA-mediated anti-leukemic activity though SUMO2/3 pathway.
- 22 February 2018
- Published by Springer Nature in Oncogene
- Vol. 37 (19) , 2559-2572
Open AccessThe HDAC inhibitor SAHA regulates CBX2 stability via a SUMO-triggered ubiquitin-mediated pathway in leukemia
Polycomb group (PcG) proteins regulate transcription, playing a key role in stemness and differentiation. Deregulation of PcG members is known to be involved in cancer pathogenesis. Emerging evidence suggests that CBX2, a member of the PcG protein family, is overexpressed in several human tumors, correlating with lower overall survival. Unraveling the mechanisms regulating CBX2 expression may thus provide a promising new target for anticancer strategies. Here we show that the HDAC inhibitor SAHA regulates CBX2 stability via a SUMO-triggered ubiquitin-mediated pathway in leukemia. We identify CBX4 and RNF4 as the E3 SUMO and E3 ubiquitin ligase, respectively, and describe the specific molecular mechanism regulating CBX2 protein stability. Finally, we show that CBX2-depleted leukemic cells display impaired proliferation, underscoring its critical role in regulating leukemia cell tumorogenicity. Our results show that SAHA affects CBX2 stability, revealing a potential SAHA-mediated anti-leukemic activity though SUMO2/3 pathway.