PXD083540

PXD083540 is an original dataset announced via ProteomeXchange.

Title	Bifunctional Titanium-based magnetic nanomaterials for simultaneous phosphoproteome and glycoproteome profiling in aging Caenorhabditis elegans
Description	Caenorhabditis elegans (C. elegans) is an exceptionally valuable model organism for aging research, where proteome remodeling is central to lifespan regulation. As two of the most typical and extensively investigated post-translational modifications (PTMs), protein phosphorylation and N-glycosylation are integral to complex biology processes closely related to aging. However, comprehensive and simultaneous profiling of the phosphoproteome and glycoproteome in the complex biological samples remains a significant technical challenge. Herein, we develop a bifunctional magnetic nanomaterial fabricated by sequential decoration of generation 5 polyamidoamine dendrimers (G5 PAMAM), phytic acid (PA) and Ti4+ ion on magnetic core (denoted as Fe3O4@PAMAM@PA-Ti4+), enabling one-step simultaneous enrichment of phosphopeptides and glycopeptides. Benefiting from its high loading of Ti4+ and abundant hydrophilic hydroxyl/amino groups, this nanomaterial demonstrated outstanding performance for phosphopeptide and glycopeptide enrichment, including excellent selectivity, high sensitivity and rapid magnetic responsiveness. Application of this bifunctional material to the C. elegans aging model allowed us to simultaneously identify 4241 phosphopeptides (from 1776 phosphoproteins) and 495 N-glycopeptides (from 349 glycoproteins) across three developmental time points (day 1, 4, and 10). Quantitative analysis revealed that some phosphoproteins were involved in aging-associated signaling, such as mTOR, insulin/IGF-1 and DAF-16/FOXO, exhibiting significant age-dependent up- or down-regulation. In contrast, the age-altered glycoproteome was predominantly related to glycolysis pathways and sarcomere stability. Notably, Unbiased clustering analysis highlighted that biphasic protein clusters exhibit a stronger correlation with the aging process compared to monotonic groups. Furthermore, dually modified (phosphorylated and glycosylated) members of the Vitellogenin (vit) family were identified as key proteins closely associated with aging. This work opens a new avenue for dual PTM analysis and provides the first comprehensive characterization of phosphoproteome and glycoproteome during C. elegans aging.
HostingRepository	iProX
AnnounceDate	2026-09-02
AnnouncementXML	Submission_2026-09-02_01:13:19.596.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Yingyue Wang
SpeciesList	scientific name: Caenorhabditis elegans; NCBI TaxID: 6239;
ModificationList	phosphorylated residue
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2026-09-02 01:13:01	ID requested
⏵ 1	2026-09-02 01:13:20	announced

Dataset with its publication pending

submitter keyword: nanomaterial, phosphorylation, glycosylation, proteomics, Caenorhabditis elegans, aging

Mingxia Gao
contact affiliation	Fudan University
contact email	mxgao@fudan.edu.cn
lab head
Yingyue Wang
contact affiliation	Fudan University
contact email	24210220032@m.fudan.edu.cn
dataset submitter

iProX dataset URI