Dataset Information

Early Secretory Pathway glycoprotein analysis dataset

ABSTRACT: Protein misfolding is one of the causes for several diseases and as a consequence, analysis of the misfolded protein fraction is one of the major aims in translational research. Here, we report a workflow and its associated dataset which focuses on the analysis of the Early Secretory Pathway (ESP) glycoproteins (gESP) from melanoma cells. Our results provide an overview on the ESP glycoprotein members by analysis of both the peptide and glycan chains. Moreover we provide the quantitative analysis of cells treated with kifunensine (an immunomodulatory agent), which blocks class I mannosidases processing of the misfolded or unfolded glycoproteins sent to degradation. Our dataset provides an overview of the major cargo of ESP glycoproteins, underpinning novel candidates for glycoprotein-related Endoplasmic Reticulum Associated Degradation (ERAD) which could be involved in melanoma antigen presentation.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Melanocyte

DISEASE(S): Melanoma

SUBMITTER: Cristian Munteanu

LAB HEAD: Ștefana M. Petrescu

PROVIDER: PXD035541 | Pride | 2023-01-31

REPOSITORIES: Pride

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Publications

Defining the altered glycoproteomic space of the early secretory pathway by class I mannosidase pharmacological inhibition.

Munteanu Cristian V A CVA Chirițoiu Gabriela N GN Petrescu Andrei-Jose AJ Petrescu Ștefana M ȘM

Frontiers in molecular biosciences 20230109

N-glycosylation is a key process for various biological functions like protein folding, maturation and sorting for the conventional secretory compartment, cell-cell communication and immune response. This is usually accomplished by a complex system of mannosidases in which those from class I have an outstanding role, commonly involved in the early protein sorting associated to the Endoplasmic Reticulum (ER) in the N-glycan dependent quality control (ERQC) and ER-associated degradation (ERAD). Al ...[more]

PMID: 36699698

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Project description:Protein 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.

Dataset Information

Early Secretory Pathway glycoprotein analysis dataset

Publications

Defining the altered glycoproteomic space of the early secretory pathway by class I mannosidase pharmacological inhibition.

Similar Datasets

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