{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wan C"],"funding":["HHS | National Institutes of Health","HHS | National Institutes of Health (NIH)","NIDDK NIH HHS","NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["e2409341121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11348294"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(34)"],"pubmed_abstract":["Vesicular transport relies on multimeric trafficking complexes to capture cargo and drive vesicle budding and fusion. Faithful assembly of the trafficking complexes is essential to their functions but remains largely unexplored. Assembly of AP2 adaptor, a heterotetrameric protein complex regulating clathrin-mediated endocytosis, is assisted by the chaperone AAGAB. Here, we found that AAGAB initiates AP2 assembly by stabilizing its α and σ2 subunits, but the AAGAB:α:σ2 complex cannot recruit additional AP2 subunits. We identified CCDC32 as another chaperone regulating AP2 assembly. CCDC32 recognizes the AAGAB:α:σ2 complex, and its binding leads to the formation of an α:σ2:CCDC32 ternary complex. The α:σ2:CCDC32 complex serves as a template that sequentially recruits the µ2 and β2 subunits o"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["An AAGAB-to-CCDC32 handover mechanism controls the assembly of the AP2 adaptor complex."],"pmcid":["PMC11348294"],"funding_grant_id":["R03 AI178109","R03 AI151651","R35 GM126960","GM138685","R01 DK124431","GM126960","R01 GM138685","DK124431"],"pubmed_authors":["Wan C","Wu J","Shen J","Li S","Tian Y","Yin Q","Puscher H","Ouyang Y"],"additional_accession":[]},"is_claimable":false,"name":"An AAGAB-to-CCDC32 handover mechanism controls the assembly of the AP2 adaptor complex.","description":"Vesicular transport relies on multimeric trafficking complexes to capture cargo and drive vesicle budding and fusion. Faithful assembly of the trafficking complexes is essential to their functions but remains largely unexplored. Assembly of AP2 adaptor, a heterotetrameric protein complex regulating clathrin-mediated endocytosis, is assisted by the chaperone AAGAB. Here, we found that AAGAB initiates AP2 assembly by stabilizing its α and σ2 subunits, but the AAGAB:α:σ2 complex cannot recruit additional AP2 subunits. We identified CCDC32 as another chaperone regulating AP2 assembly. CCDC32 recognizes the AAGAB:α:σ2 complex, and its binding leads to the formation of an α:σ2:CCDC32 ternary complex. The α:σ2:CCDC32 complex serves as a template that sequentially recruits the µ2 and β2 subunits o","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2025-04-26T21:58:11.629Z","creation":"2025-04-06T17:00:27.152Z"},"accession":"S-EPMC11348294","cross_references":{"pubmed":["39145939"],"doi":["10.1073/pnas.2409341121"]}}