{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Allegre J"],"funding":["Ligue Contre le Cancer","Conseil Régional de Bourgogne","Agence Nationale de la Recherche","Fondation pour la Recherche Médicale","Ministère de l’Enseignement supérieur, de la Recherche et de l’Innovation"],"pagination":["e0206253"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6201919"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(10)"],"pubmed_abstract":["The cellular inhibitor of apoptosis 1 (cIAP1) is an E3-ubiquitin ligase that regulates cell signaling pathways involved in fundamental cellular processes including cell death, cell proliferation, cell differentiation and inflammation. It recruits ubiquitination substrates thanks to the presence of three baculoviral IAP repeat (BIR) domains at its N-terminal extremity. We previously demonstrated that cIAP1 promoted the ubiquitination of the E2 factor 1 (E2F1) transcription factor. Moreover, we showed that cIAP1 was required for E2F1 stabilization during the S phase of cell cycle and in response to DNA damage. Here, we report that E2F1 binds within the cIAP1 BIR3 domain. The BIR3 contains a surface hydrophobic groove that specifically anchors a conserved IAP binding motif (IBM) found in a nu"],"journal":["PloS one"],"pubmed_title":["E2F1 binds to the peptide-binding groove within the BIR3 domain of cIAP1 and requires cIAP1 for chromatin binding."],"pmcid":["PMC6201919"],"funding_grant_id":["ANR-11-LABX-0021"],"pubmed_authors":["Maillet L","Kayaci C","Berthelet J","Dubrez L","Droin N","Allegre J","Cartier J","Dumetier B","Vuillier C","Glorian V","Gemble S","Garrido C"],"additional_accession":[]},"is_claimable":false,"name":"E2F1 binds to the peptide-binding groove within the BIR3 domain of cIAP1 and requires cIAP1 for chromatin binding.","description":"The cellular inhibitor of apoptosis 1 (cIAP1) is an E3-ubiquitin ligase that regulates cell signaling pathways involved in fundamental cellular processes including cell death, cell proliferation, cell differentiation and inflammation. It recruits ubiquitination substrates thanks to the presence of three baculoviral IAP repeat (BIR) domains at its N-terminal extremity. We previously demonstrated that cIAP1 promoted the ubiquitination of the E2 factor 1 (E2F1) transcription factor. Moreover, we showed that cIAP1 was required for E2F1 stabilization during the S phase of cell cycle and in response to DNA damage. Here, we report that E2F1 binds within the cIAP1 BIR3 domain. The BIR3 contains a surface hydrophobic groove that specifically anchors a conserved IAP binding motif (IBM) found in a nu","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018","modification":"2026-06-11T03:20:17.749Z","creation":"2019-03-27T00:07:36Z"},"accession":"S-EPMC6201919","cross_references":{"pubmed":["30359437"],"doi":["10.1371/journal.pone.0206253"]}}