{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["24(8)"],"submitter":["Scalia P"],"pubmed_abstract":["EphB4 angiogenic kinase over-expression in Mesothelioma cells relies upon a degradation rescue signal provided by autocrine IGF-II activation of Insulin Receptor A. However, the identity of the molecular machinery involved in EphB4 rapid degradation upon IGF-II signal deprivation are unknown. Using targeted proteomics, protein-protein interaction methods, PCR cloning, and 3D modeling approaches, we identified a novel ubiquitin E3 ligase complex recruited by the EphB4 C tail upon autocrine IGF-II signal deprivation. We show this complex to contain a previously unknown N-Terminal isoform of Deltex3 E3-Ub ligase (referred as \"DTX3c\"), along with UBA1(E1) and UBE2N(E2) ubiquitin ligases and the ATPase/unfoldase Cdc48/p97. Upon autocrine IGF-II neutralization in cultured MSTO211H (a Malignant M"],"journal":["International journal of molecular sciences"],"pagination":["7380"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10139083"],"repository":["biostudies-literature"],"pubmed_title":["Novel Isoform DTX3c Associates with UBE2N-UBA1 and Cdc48/p97 as Part of the EphB4 Degradation Complex Regulated by the Autocrine IGF-II/IR<sup>A</sup> Signal in Malignant Mesothelioma."],"pmcid":["PMC10139083"],"pubmed_authors":["Scalia P","Carnevale V","Suma A","Merali C","Merali S","Williams SJ","Barrero C"],"additional_accession":[]},"is_claimable":false,"name":"Novel Isoform DTX3c Associates with UBE2N-UBA1 and Cdc48/p97 as Part of the EphB4 Degradation Complex Regulated by the Autocrine IGF-II/IR<sup>A</sup> Signal in Malignant Mesothelioma.","description":"EphB4 angiogenic kinase over-expression in Mesothelioma cells relies upon a degradation rescue signal provided by autocrine IGF-II activation of Insulin Receptor A. However, the identity of the molecular machinery involved in EphB4 rapid degradation upon IGF-II signal deprivation are unknown. Using targeted proteomics, protein-protein interaction methods, PCR cloning, and 3D modeling approaches, we identified a novel ubiquitin E3 ligase complex recruited by the EphB4 C tail upon autocrine IGF-II signal deprivation. We show this complex to contain a previously unknown N-Terminal isoform of Deltex3 E3-Ub ligase (referred as \"DTX3c\"), along with UBA1(E1) and UBE2N(E2) ubiquitin ligases and the ATPase/unfoldase Cdc48/p97. Upon autocrine IGF-II neutralization in cultured MSTO211H (a Malignant M","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Apr","modification":"2026-04-07T17:34:51.268Z","creation":"2024-10-18T18:31:12.456Z"},"accession":"S-EPMC10139083","cross_references":{"pubmed":["37108544"],"doi":["10.3390/ijms24087380"]}}