PXD009199 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Mapping Ubiquitination Sites in Alzheimer's Disease |
Description | Alzheimer’s Disease (AD) is characterized by the deposition of protein aggregates such as neurofibrillary tangles (NFTs) and amyloid (Aβ) plaques in the brain. Post-translational modification through ubiquitylationplays critical roles in clearing misfolded protein aggregates. Investigating global ubiquitylation changes inAD brain may provide insights regarding the underlying mechanisms of proteostasis and disease pathogenesis.Here, we utilizedan immunoaffinity approach to specifically enrichubiquitinated(di-glycine) peptides frompostmortemhuman control and AD braintissues.Mass spectrometry(MS)based proteomicanalysis identified global ubiquitylation changes associated with ADand hierarchical clustering of the human brain ubiquitylome clearly classified AD cases from healthy controls based on ubiquitylation patterns. Polyubiquitin linkage analysis identified increased levels of all seven polyubiquitin linkage typesas well as total ubiquitin in the AD brain tissues.We also report novel ubiquitylation sites in the microtubulebinding repeatof Tauwith potential implicationsfor Tauaggregation. Dually modified peptides with both phosphorylation and ubiquitylationsites, many of which originated from Tauprotein are also differentially enriched in AD.Furthermore, all the KXGS motifswithin themicrotubule binding region (MTBR)of Tauprotein,which represents the core ofNFTs,are enriched among dually modified peptides. Collectively, these studieshighlight the utility of an immunoaffinity enrichment approach coupled with MSanalysis for mapping AD associated global ubiquitylome changesas well as to gain insights intounderlying proteostasis pathwaysaltered in AD brain. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:43:43.676.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Eric Dammer |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | ubiquitination signature dipeptidyl lysine; phosphorylated residue |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-03-13 08:18:12 | ID requested | |
1 | 2019-06-25 03:18:22 | announced | |
⏵ 2 | 2024-10-22 04:43:51 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1002/pmic.201800108; |
Abreha MH, Dammer EB, Ping L, Zhang T, Duong DM, Gearing M, Lah JJ, Levey AI, Seyfried NT, Quantitative Analysis of the Brain Ubiquitylome in Alzheimer's Disease. Proteomics, 18(20):e1800108(2018) [pubmed] |
Keyword List
curator keyword: Biological, Biomedical |
submitter keyword: ubiquitylome,AD, GG remnant peptides |
Contact List
Nicholas T. Seyfried |
contact affiliation | Emory University School of Medicine Department of Biochemistry |
contact email | nseyfri@emory.edu |
lab head | |
Eric Dammer |
contact affiliation | Emory University |
contact email | edammer@emory.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/06/PXD009199 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD009199
- Label: PRIDE project
- Name: Mapping Ubiquitination Sites in Alzheimer's Disease