{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wirth M"],"funding":["Cancer Research UK","The Francis Crick Institute","Wellcome Trust"],"pagination":["2055"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6499816"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_abstract":["Autophagy is an essential recycling and quality control pathway. Mammalian ATG8 proteins drive autophagosome formation and selective removal of protein aggregates and organelles by recruiting autophagy receptors and adaptors that contain a LC3-interacting region (LIR) motif. LIR motifs can be highly selective for ATG8 subfamily proteins (LC3s/GABARAPs), however the molecular determinants regulating these selective interactions remain elusive. Here we show that residues within the core LIR motif and adjacent C-terminal region as well as ATG8 subfamily-specific residues in the LIR docking site are critical for binding of receptors and adaptors to GABARAPs. Moreover, rendering GABARAP more LC3B-like impairs autophagy receptor degradation. Modulating LIR binding specificity of the centriolar s"],"journal":["Nature communications"],"pubmed_title":["Molecular determinants regulating selective binding of autophagy adapters and receptors to ATG8 proteins."],"pmcid":["PMC6499816"],"funding_grant_id":["15153","FC001999","10187","10013","FC001187","10015"],"pubmed_authors":["Zhang W","Wirth M","Razi M","Johansen T","O'Reilly N","Tooze SA","Nyoni L","Mouilleron S","Joshi D"],"additional_accession":[]},"is_claimable":false,"name":"Molecular determinants regulating selective binding of autophagy adapters and receptors to ATG8 proteins.","description":"Autophagy is an essential recycling and quality control pathway. Mammalian ATG8 proteins drive autophagosome formation and selective removal of protein aggregates and organelles by recruiting autophagy receptors and adaptors that contain a LC3-interacting region (LIR) motif. LIR motifs can be highly selective for ATG8 subfamily proteins (LC3s/GABARAPs), however the molecular determinants regulating these selective interactions remain elusive. Here we show that residues within the core LIR motif and adjacent C-terminal region as well as ATG8 subfamily-specific residues in the LIR docking site are critical for binding of receptors and adaptors to GABARAPs. Moreover, rendering GABARAP more LC3B-like impairs autophagy receptor degradation. Modulating LIR binding specificity of the centriolar s","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 May","modification":"2026-05-04T21:10:36.308Z","creation":"2025-05-29T22:10:17.588Z"},"accession":"S-EPMC6499816","cross_references":{"pubmed":["31053714"],"doi":["10.1038/s41467-019-10059-6"]}}