{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Welch LG"],"funding":["MRC Laboratory of Molecular Biology","Medical Research Council"],"pagination":["jcs262160"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11441981"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["137(17)"],"pubmed_abstract":["Golgi-resident enzymes remain in place while their substrates flow through from the endoplasmic reticulum to elsewhere in the cell. COPI-coated vesicles bud from the Golgi to recycle Golgi residents to earlier cisternae. Different enzymes are present in different parts of the stack, and one COPI adaptor protein, GOLPH3, acts to recruit enzymes into vesicles in part of the stack. Here, we used proximity biotinylation to identify further components of intra-Golgi vesicles and found FAM114A2, a cytosolic protein. Affinity chromatography with FAM114A2, and its paralogue FAM114A1, showed that they bind to Golgi-resident membrane proteins, with membrane-proximal basic residues in the cytoplasmic tail being sufficient for the interaction. Deletion of both proteins from U2OS cells did not cause su"],"journal":["Journal of cell science"],"pubmed_title":["The FAM114A proteins are adaptors for the recycling of Golgi enzymes."],"pmcid":["PMC11441981"],"funding_grant_id":["MC_U105178783"],"pubmed_authors":["Welch LG","Muschalik N","Munro S"],"additional_accession":[]},"is_claimable":false,"name":"The FAM114A proteins are adaptors for the recycling of Golgi enzymes.","description":"Golgi-resident enzymes remain in place while their substrates flow through from the endoplasmic reticulum to elsewhere in the cell. COPI-coated vesicles bud from the Golgi to recycle Golgi residents to earlier cisternae. Different enzymes are present in different parts of the stack, and one COPI adaptor protein, GOLPH3, acts to recruit enzymes into vesicles in part of the stack. Here, we used proximity biotinylation to identify further components of intra-Golgi vesicles and found FAM114A2, a cytosolic protein. Affinity chromatography with FAM114A2, and its paralogue FAM114A1, showed that they bind to Golgi-resident membrane proteins, with membrane-proximal basic residues in the cytoplasmic tail being sufficient for the interaction. Deletion of both proteins from U2OS cells did not cause su","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Sep","modification":"2026-06-01T06:58:03.974Z","creation":"2025-04-04T01:37:18.271Z"},"accession":"S-EPMC11441981","cross_references":{"pubmed":["39129673"],"doi":["10.1242/jcs.262160"]}}