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dc.contributor.authorCollins, MO
dc.contributor.authorWoodley, KT
dc.contributor.authorChoudhary, JS
dc.date.accessioned2020-10-15T15:34:03Z
dc.date.issued2017-07-05
dc.identifier.citationScientific reports, 2017, 7 (1), pp. 4683 - ?
dc.identifier.issn2045-2322
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/4163
dc.identifier.eissn2045-2322
dc.identifier.doi10.1038/s41598-017-04580-1
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.
dc.formatElectronic
dc.format.extent4683 - ?
dc.languageeng
dc.language.isoeng
dc.publisherNATURE PUBLISHING GROUP
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectProsencephalon
dc.subjectAnimals
dc.subjectMice
dc.subjectProteins
dc.subjectProteomics
dc.subjectAcylation
dc.subjectPhosphorylation
dc.subjectMass Spectrometry
dc.titleGlobal, site-specific analysis of neuronal protein S-acylation.
dc.typeJournal Article
dcterms.dateAccepted2017-05-17
rioxxterms.versionofrecord10.1038/s41598-017-04580-1
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2017-07-05
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfScientific reports
pubs.issue1
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR
pubs.publication-statusPublished
pubs.volume7
pubs.embargo.termsNot known
dc.contributor.icrauthorChoudhary, Jyoti


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