{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wallace NS"],"funding":["NEI NIH HHS","NIDDK NIH HHS","NIMH NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["ar56"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11064669"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["35(4)"],"pubmed_abstract":["Tepsin is an established accessory protein found in Adaptor Protein 4 (AP-4) coated vesicles, but the biological role of tepsin remains unknown. AP-4 vesicles originate at the <i>trans</i>-Golgi network (TGN) and target the delivery of ATG9A, a scramblase required for autophagosome biogenesis, to the cell periphery. Using in silico methods, we identified a putative <u>L</u>C3-<u>I</u>nteracting <u>R</u>egion (LIR) motif in tepsin. Biochemical experiments using purified recombinant proteins indicate tepsin directly binds LC3B preferentially over other members of the mammalian ATG8 family. Calorimetry and structural modeling data indicate this interaction occurs with micromolar affinity using the established LC3B LIR docking site. Loss of tepsin in cultured cells dysregulates ATG9A export fr"],"journal":["Molecular biology of the cell"],"pubmed_title":["Tepsin binds LC3B to promote ATG9A trafficking and delivery."],"pmcid":["PMC11064669"],"funding_grant_id":["P30 DK020593","P30 CA068485","T32 GM008320","R35 GM119525","U24 DK059637","P30 DK058404","T32 MH065215","P30 EY008126"],"pubmed_authors":["Jackson LP","Kendall AK","Wallace NS","Gadbery JE","Cohen CI"],"additional_accession":[]},"is_claimable":false,"name":"Tepsin binds LC3B to promote ATG9A trafficking and delivery.","description":"Tepsin is an established accessory protein found in Adaptor Protein 4 (AP-4) coated vesicles, but the biological role of tepsin remains unknown. AP-4 vesicles originate at the <i>trans</i>-Golgi network (TGN) and target the delivery of ATG9A, a scramblase required for autophagosome biogenesis, to the cell periphery. Using in silico methods, we identified a putative <u>L</u>C3-<u>I</u>nteracting <u>R</u>egion (LIR) motif in tepsin. Biochemical experiments using purified recombinant proteins indicate tepsin directly binds LC3B preferentially over other members of the mammalian ATG8 family. Calorimetry and structural modeling data indicate this interaction occurs with micromolar affinity using the established LC3B LIR docking site. Loss of tepsin in cultured cells dysregulates ATG9A export fr","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-06-03T03:58:50.74Z","creation":"2026-04-24T03:09:52.866Z"},"accession":"S-EPMC11064669","cross_references":{"pubmed":["38381558"],"doi":["10.1091/mbc.E23-09-0359-T"]}}