{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gross A"],"funding":["Deutsche Forschungsgemeinschaft","European Research Council","Max-Planck-Gesellschaft"],"pagination":["978-994"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7616460"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["598(9)"],"pubmed_abstract":["Patients with Skraban-Deardorff syndrome (SKDEAS), a neurodevelopmental syndrome associated with a spectrum of developmental and intellectual delays and disabilities, harbor diverse mutations in WDR26, encoding a subunit of the multiprotein CTLH E3 ubiquitin ligase complex. Structural studies revealed that homodimers of WDR26 bridge two core-CTLH E3 complexes to generate giant, hollow oval-shaped supramolecular CTLH E3 assemblies. Additionally, WDR26 mediates CTLH E3 complex binding to subunit YPEL5 and functions as substrate receptor for the transcriptional repressor HBP1. Here, we mapped SKDEAS-associated mutations on a WDR26 structural model and tested their functionality in complementation studies using genetically engineered human cells lacking CTLH E3 supramolecular assemblies. Despi"],"journal":["FEBS letters"],"pubmed_title":["Skraban-Deardorff intellectual disability syndrome-associated mutations in WDR26 impair CTLH E3 complex assembly."],"pmcid":["PMC7616460"],"funding_grant_id":["SCHU 3196/1‐1","101098161","SCHU 3196/1-1","UPSmeetMET,10109816"],"pubmed_authors":["Gross A","Chrustowicz J","Murray PJ","Schulman BA","Sherpa D","Strasser A","Alpi AF","Gottemukkala KV","Muller J"],"additional_accession":[]},"is_claimable":false,"name":"Skraban-Deardorff intellectual disability syndrome-associated mutations in WDR26 impair CTLH E3 complex assembly.","description":"Patients with Skraban-Deardorff syndrome (SKDEAS), a neurodevelopmental syndrome associated with a spectrum of developmental and intellectual delays and disabilities, harbor diverse mutations in WDR26, encoding a subunit of the multiprotein CTLH E3 ubiquitin ligase complex. Structural studies revealed that homodimers of WDR26 bridge two core-CTLH E3 complexes to generate giant, hollow oval-shaped supramolecular CTLH E3 assemblies. Additionally, WDR26 mediates CTLH E3 complex binding to subunit YPEL5 and functions as substrate receptor for the transcriptional repressor HBP1. Here, we mapped SKDEAS-associated mutations on a WDR26 structural model and tested their functionality in complementation studies using genetically engineered human cells lacking CTLH E3 supramolecular assemblies. Despi","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-02T06:31:22.456Z","creation":"2025-04-04T09:58:53.587Z"},"accession":"S-EPMC7616460","cross_references":{"pubmed":["38575527"],"doi":["10.1002/1873-3468.14866"]}}