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The substrates of PPT1 are largely undescribed, posing a limitation on molecular dissection of disease mechanisms and therapeutic development. Here, we provide a resource identifying &gt;100 novel PPT1 substrates. We utilized Acyl Resin-Assisted Capture (Acyl RAC) and mass spectrometry to identify proteins with increased\n                    <jats:italic>in vivo<\/jats:italic>\n                    palmitoylation in PPT1 knockout (KO) mouse brains. We then validated putative substrates through direct depalmitoylation with recombinant PPT1. This stringent screen elucidated diverse PPT1 substrates at the synapse, including channels and transporters, G-protein\u2013associated molecules, endo\/exocytic components, synaptic adhesion molecules, and mitochondrial proteins. Cysteine depalmitoylation sites in transmembrane PPT1 substrates frequently participate in disulfide bonds in the mature protein. We confirmed that depalmitoylation plays a role in disulfide bond formation in a tertiary screen analyzing posttranslational modifications (PTMs). Collectively, these data highlight the role of PPT1 in mediating synapse functions, implicate molecular pathways in the etiology of NCL and other neurodegenerative diseases, and advance our basic understanding of the purpose of depalmitoylation.\n                  <\/jats:p>","DOI":"10.1371\/journal.pbio.3001590","type":"journal-article","created":{"date-parts":[[2022,3,31]],"date-time":"2022-03-31T14:11:18Z","timestamp":1648735878000},"page":"e3001590","update-policy":"https:\/\/doi.org\/10.1371\/journal.pbio.corrections_policy","source":"Crossref","is-referenced-by-count":60,"title":["Identification of substrates of palmitoyl protein thioesterase 1\u00a0highlights roles of depalmitoylation in disulfide bond formation and synaptic function"],"prefix":"10.1371","volume":"20","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0542-3793","authenticated-orcid":true,"given":"Erica L.","family":"Gorenberg","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7545-411X","authenticated-orcid":true,"given":"Sofia","family":"Massaro Tieze","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bet\u00fcl","family":"Y\u00fccel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Helen R.","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vicky","family":"Chou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9645-1882","authenticated-orcid":true,"given":"Gregory S.","family":"Wirak","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susumu","family":"Tomita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"TuKiet T.","family":"Lam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sreeganga S.","family":"Chandra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2022,3,31]]},"reference":[{"key":"pbio.3001590.ref001","doi-asserted-by":"crossref","first-page":"3353","DOI":"10.1002\/j.1460-2075.1987.tb02656.x","article-title":"Dynamic fatty acylation of p21N-ras","volume":"6","author":"AI Magee","year":"1987","journal-title":"EMBO J"},{"key":"pbio.3001590.ref002","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1042\/BST20140270","article-title":"The zDHHC family of S-acyltransferases","volume":"43","author":"K Lemonidis","year":"2015","journal-title":"Biochem Soc Trans"},{"key":"pbio.3001590.ref003","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1194\/jlr.R600007-JLR200","article-title":"Thematic review series: Lipid Posttranslational Modifications. 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