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PXD053367

PXD053367 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleA pilot study for deciphering post-translational modifications and proteoforms of tau protein by capillary electrophoresis-mass spectrometry
DescriptionAbnormal accumulation of tau proteins is one pathological hallmark of Alzheimer’s disease (AD). Many tau protein post-translational modifications (PTMs) are associated with the development of AD, such as phosphorylation, acetylation, and methylation. Therefore, a complete picture of PTM landscape of tau is critical for understanding the molecular mechanisms of AD progression. Here, we offered a pilot study of combining two complementary analytical techniques, capillary zone electrophoresis (CZE)-tandem mass spectrometry (MS/MS) and reversed-phase liquid chromatography (RPLC)-MS/MS, for bottom-up proteomics of tau-0N3R. We identified 53 phosphorylation sites of tau-0N3R in total, which is about 30% higher than that from RPLC-MS/MS alone. CZE-MS/MS provided more PTM sites (i.e., phosphorylation) and modified peptides of tau-0N3R than RPLC-MS/MS, and its predicted electrophoretic mobility helped improve the confidence of the identified modified peptides. We developed a highly efficient capillary isoelectric focusing (cIEF)-MS technique to offer a bird’s-eye view of tau-0N3R proteoforms, with 11 putative tau-0N3R proteoforms carrying up to ten phosphorylation sites and lower pI values from more phosphorylated proteoforms detected. Interestingly, under a native-like cIEF-MS condition, we observed three putative tau-0N3R dimers carrying phosphate groups. The findings demonstrate that CE-MS is a valuable analytical technique for the characterization of tau PTMs, proteoforms, and even oligomerization.
HostingRepositoryPRIDE
AnnounceDate2024-10-15
AnnouncementXMLSubmission_2024-10-15_05:16:56.134.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterLiangliang Sun
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListphosphorylated residue; acetylated residue
InstrumentQ Exactive HF
Dataset History
RevisionDatetimeStatusChangeLog Entry
02024-06-24 10:52:18ID requested
12024-10-15 05:16:57announced
Publication List
Fang F, Xu T, Chien Hagar HT, Hovde S, Kuo MH, Sun L, Pilot Study for Deciphering Post-Translational Modifications and Proteoforms of Tau Protein by Capillary Electrophoresis-Mass Spectrometry. J Proteome Res, ():(2024) [pubmed]
10.1021/acs.jproteome.4c00587;
Keyword List
submitter keyword: Alzheimer’s disease, capillary electrophoresis-mass spectrometry, post-translational modification,Tau protein, phosphorylation, proteoform
Contact List
Liangliang Sun
contact affiliationDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, MI 48824, United States.
contact emaillsun@chemistry.msu.edu
lab head
Liangliang Sun
contact affiliationMichigan State University
contact emaillsun@chemistry.msu.edu
dataset submitter
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Dataset FTP location
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