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dc.contributor.authorCollins, MOen_US
dc.contributor.authorWoodley, KTen_US
dc.contributor.authorChoudhary, JSen_US
dc.date.accessioned2020-10-15T15:34:03Z
dc.date.issued2017-07-05en_US
dc.identifier.citationScientific reports, 2017, 7 (1), pp. 4683 - ?en_US
dc.identifier.issn2045-2322en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/4163
dc.identifier.eissn2045-2322en_US
dc.identifier.doi10.1038/s41598-017-04580-1en_US
dc.description.abstractProtein S-acylation (palmitoylation) is a reversible lipid modification that is an important regulator of dynamic membrane-protein interactions. Proteomic approaches have uncovered many putative palmitoylated proteins however, methods for comprehensive palmitoylation site characterization are lacking. We demonstrate a quantitative site-specific-Acyl-Biotin-Exchange (ssABE) method that allowed the identification of 906 putative palmitoylation sites on 641 proteins from mouse forebrain. 62% of sites map to known palmitoylated proteins and 102 individual palmitoylation sites are known from the literature. 54% of palmitoylation sites map to synaptic proteins including many GPCRs, receptors/ion channels and peripheral membrane proteins. Phosphorylation sites were also identified on a subset of peptides that were palmitoylated, demonstrating for the first time co-identification of these modifications by mass spectrometry. Palmitoylation sites were identified on over half of the family of palmitoyl-acyltransferases (PATs) that mediate protein palmitoylation, including active site thioester-linked palmitoyl intermediates. Distinct palmitoylation motifs and site topology were identified for integral membrane and soluble proteins, indicating potential differences in associated PAT specificity and palmitoylation function. ssABE allows the global identification of palmitoylation sites as well as measurement of the active site modification state of PATs, enabling palmitoylation to be studied at a systems level.en_US
dc.formatElectronicen_US
dc.format.extent4683 - ?en_US
dc.languageengen_US
dc.language.isoengen_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en_US
dc.subjectProsencephalonen_US
dc.subjectAnimalsen_US
dc.subjectMiceen_US
dc.subjectProteinsen_US
dc.subjectProteomicsen_US
dc.subjectAcylationen_US
dc.subjectPhosphorylationen_US
dc.subjectMass Spectrometryen_US
dc.titleGlobal, site-specific analysis of neuronal protein S-acylation.en_US
dc.typeJournal Article
dcterms.dateAccepted2017-05-17en_US
rioxxterms.versionofrecord10.1038/s41598-017-04580-1en_US
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0en_US
rioxxterms.licenseref.startdate2017-07-05en_US
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfScientific reportsen_US
pubs.issue1en_US
pubs.notesNot knownen_US
pubs.organisational-group/ICR
pubs.publication-statusPublisheden_US
pubs.volume7en_US
pubs.embargo.termsNot knownen_US
dc.contributor.icrauthorChoudhary, Jyotien_US


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