{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Abrami L"],"funding":["Swiss National Science Foundation","European Research Council"],"pagination":["438-447"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7610442"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(4)"],"pubmed_abstract":["Many biochemical reactions require controlled recruitment of proteins to membranes. This is largely regulated by posttranslational modifications. A frequent one is S-acylation, which consists of the addition of acyl chains and can be reversed by poorly understood acyl protein thioesterases (APTs). Using a panel of computational and experimental approaches, we dissect the mode of action of the major cellular thioesterase APT2 (LYPLA2). We show that soluble APT2 is vulnerable to proteasomal degradation, from which membrane binding protects it. Interaction with membranes requires three consecutive steps: electrostatic attraction, insertion of a hydrophobic loop and S-acylation by the palmitoyltransferases ZDHHC3 or ZDHHC7. Once bound, APT2 is predicted to deform the lipid bilayer to extract t"],"journal":["Nature chemical biology"],"pubmed_title":["Palmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains."],"pmcid":["PMC7610442"],"funding_grant_id":["176393","340260","192608"],"pubmed_authors":["Marcaida MJ","Fonti G","Dal Peraro M","Ho S","Anwar MU","Abrami L","Sandoz PA","van der Goot FG","Audagnotto M","Mesquita FS","Pojer F"],"additional_accession":[]},"is_claimable":false,"name":"Palmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains.","description":"Many biochemical reactions require controlled recruitment of proteins to membranes. This is largely regulated by posttranslational modifications. A frequent one is S-acylation, which consists of the addition of acyl chains and can be reversed by poorly understood acyl protein thioesterases (APTs). Using a panel of computational and experimental approaches, we dissect the mode of action of the major cellular thioesterase APT2 (LYPLA2). We show that soluble APT2 is vulnerable to proteasomal degradation, from which membrane binding protects it. Interaction with membranes requires three consecutive steps: electrostatic attraction, insertion of a hydrophobic loop and S-acylation by the palmitoyltransferases ZDHHC3 or ZDHHC7. Once bound, APT2 is predicted to deform the lipid bilayer to extract t","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2026-04-18T01:30:59.641Z","creation":"2022-02-11T10:50:15.806Z"},"accession":"S-EPMC7610442","cross_references":{"pubmed":["33707782"],"doi":["10.1038/s41589-021-00753-2"]}}