<<< Full experiment listing

PXD003677

PXD003677 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe metacaspase Mca1p restricts O-glycosylation during farnesol-induced apoptosis in Candida albicans
DescriptionProtein glycolysation is an essential posttranslational modification in eukaryotic cells. In pathogenic yeasts, it is involved in a large number of biological processes, such as protein folding quality control, cell viability and host/pathogen relationships. A link between protein glycosylation and apoptosis was established by the analysis of the phenotypes of oligosaccharyltransferase mutants in budding yeast. However, little is known about the contribution of glycosylation modifications to the adaptive response to apoptosis inducers. The cysteine protease metacaspase Mca1p plays a key role in the apoptotic response in Candida albicans triggered by the quorum sensing molecule farnesol. We subjected wild-type and mca1-deletion strains to farnesol stress and then studied the early phase of apoptosis release in quantitative glycoproteomics and glycomics experiments on cell-free extracts essentially devoid of cell walls. We identified and characterized 62 new glycosylated peptides with their glycan composition: 17 N-glycosylated, 45 O-glycosylated, and 81 additional sites of N-glycosylation. The glycosylated proteins were predicted as located mostly in the “membrane” and “cell wall” compartments, but they were also related to the “nucleus” and the “mitochondrial” compartments. They were found to be involved in the control of protein folding, cell wall integrity and cell cycle regulation. We showed a general increase in the O-glycosylation of proteins in the mca1 deletion strain after farnesol challenge. We identified 44 new putative protein substrates of the metacaspase in the glycoprotein fraction enriched on concanavalin A. Most of these substrates are involved in protein folding or protein resolubilization and in mitochondrial functions. We show here that key Mca1p substrates, such as Cdc48p or Ssb1p, involved in degrading misfolded glycoproteins and in the protein quality control system, are themselves differentially glycosylated. We found putative substrates, such as Bgl2p, Srb1p or Ugp1p, that are involved in the biogenesis of glycans. We validated as a substrate of Mca1p the endo-beta-1,3-glucanase Bgl2p which is involved in the incorporation of newly synthetized mannoproteins in the cell wall. Our findings highlight a new role of the metacaspase in amplifying cell death processes by affecting several critical protein quality control systems through the alteration of the protein glycosylation machinery.
HostingRepositoryPRIDE
AnnounceDate2016-05-02
AnnouncementXMLSubmission_2016-05-02_04:16:08.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterThibaut Léger
SpeciesList scientific name: Candida albicans (Yeast); NCBI TaxID: 5476;
ModificationListphosphorylated residue; acetylated residue; complex glycosylation
InstrumentOrbitrap Fusion ETD
Dataset History
RevisionDatetimeStatusChangeLog Entry
02016-02-23 01:29:55ID requested
12016-05-02 04:16:09announced
Publication List
L, é, ger T, Garcia C, Camadro JM, The Metacaspase (Mca1p) Restricts O-glycosylation During Farnesol-induced Apoptosis in Candida albicans. Mol Cell Proteomics, 15(7):2308-23(2016) [pubmed]
Keyword List
curator keyword: Biological
submitter keyword: Candida albicans, O-glycosylation, N-glycosylation, glycans quantification, aminoxyTMT, apoptosis, farnesol, metacaspase, BGL2, CDC48, SSB1, ERAD, PDI1, glycomics, glycoproteomics, Orbitrap Fusion.
Contact List
Jean-Michel Camadro
contact affiliationMass Spectrometry Laboratory, Institut Jacques Monod, UMR 7592, Univ Paris Diderot, CNRS, Sorbonne Paris Cité, F-75205 Paris, France
contact emailjean-michel.camadro@ijm.fr
lab head
Thibaut Léger
contact affiliationInstitut Jacques Monod
contact emailleger@ijm.univ-paris-diderot.fr
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/2016/05/PXD003677
PRIDE project URI
Repository Record List
[ + ]