http://www.cnr.it/ontology/cnr/individuo/prodotto/ID309666
HIPK2 sustains apoptotic response by phosphorylating Che-1/AATF and promoting its degradation (Articolo in rivista)
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- Label
- HIPK2 sustains apoptotic response by phosphorylating Che-1/AATF and promoting its degradation (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1038/cddis.2014.381 (literal)
- Alternative label
De Nicola, F.; Catena, V.; Rinaldo, C.; Bruno, T.; Iezzi, S.; Sorino, C.; Desantis, A.; Camerini, S.; Crescenzi, M.; Floridi, A.; Passananti, C.; Soddu, S.; Fanciulli, M. (2014)
HIPK2 sustains apoptotic response by phosphorylating Che-1/AATF and promoting its degradation
in Cell death and disease
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- De Nicola, F.; Catena, V.; Rinaldo, C.; Bruno, T.; Iezzi, S.; Sorino, C.; Desantis, A.; Camerini, S.; Crescenzi, M.; Floridi, A.; Passananti, C.; Soddu, S.; Fanciulli, M. (literal)
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- Note
- ISI Web of Science (WOS) (literal)
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- Regina Elena Inst Canc Res; University of Aquila; Consiglio Nazionale delle Ricerche (CNR); Regina Elena Inst Canc Res; Istituto Superiore di Sanita'; IBPM-CNR (literal)
- Titolo
- HIPK2 sustains apoptotic response by phosphorylating Che-1/AATF and promoting its degradation (literal)
- Abstract
- Che-1/AATF is an RNA polymerase II-binding protein that is involved in the regulation of gene transcription, which undergoes stabilization and accumulation in response to DNA damage. We have previously demonstrated that following apoptotic induction, Che-1 protein levels are downregulated through its interaction with the E3 ligase HDM2, which leads to Che-1 degradation by ubiquitylation. This interaction is mediated by Pin1, which determines a phosphorylation-dependent conformational change. Here we demonstrate that HIPK2, a proapoptotic kinase, is involved in Che-1 degradation. HIPK2 interacts with Che-1 and, upon genotoxic stress, phosphorylates it at specific residues. This event strongly increases HDM2/Che-1 interaction and degradation of Che-1 protein via ubiquitin-dependent proteasomal system. In agreement with these findings, we found that HIPK2 depletion strongly decreases Che-1 ubiquitylation and degradation. Notably, Che-1 overexpression strongly counteracts HIPK2-induced apoptosis. Our results establish Che-1 as a new HIPK2 target and confirm its important role in the cellular response to DNA damage. (literal)
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