Proteomics

Dataset Information

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Global view of domain-specific O-linked mannose glycosylation in glycoengineered cells


ABSTRACT: Protein O-linked mannose (O-Man) glycosylation is an evolutionary conserved post-translational modification, whose biosynthesis is initiated by three non-redundant enzyme families, POMT1/POMT2, TMTC1-4 and TMEM260. In this study, we applied a targeted workflow for membrane glycoproteomics to five human cell lines and to a panel of genetically engineered cells with individual and combinatorial knock-out of O-Man glycosyltransferase genes to extensively map substrates, specificities, and crosstalk of O-Man enzymes. Our quantitative glycoproteomics results demonstrate new protein targets for the POMT1/POMT2 pathway and show that TMTC1-4 and TMEM260 widely target distinct Ig-like protein domains of plasma membrane proteins. This new evidence adds further knowledge on the emerging concept of domain-specific O-Man glycosylation and establishes a platform for functional studies of O-Man glycosylated adhesion molecules and receptors.

INSTRUMENT(S): Orbitrap Fusion Lumos, Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture, Diploid Cell

DISEASE(S): Colon Cancer,Disease Free,Neuroblastoma,Malignant Neoplasm Of Ovary,Liver Carcinoma

SUBMITTER: Adnan Halim  

LAB HEAD: Adnan Halim

PROVIDER: PXD045597 | Pride | 2024-06-10

REPOSITORIES: Pride

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Publications

Global View of Domain-Specific O-Linked Mannose Glycosylation in Glycoengineered Cells.

Povolo Lorenzo L   Tian Weihua W   Vakhrushev Sergey Y SY   Halim Adnan A  

Molecular & cellular proteomics : MCP 20240606 7


Protein O-linked mannose (O-Man) glycosylation is an evolutionary conserved posttranslational modification that fulfills important biological roles during embryonic development. Three nonredundant enzyme families, POMT1/POMT2, TMTC1-4, and TMEM260, selectively coordinate the initiation of protein O-Man glycosylation on distinct classes of transmembrane proteins, including α-dystroglycan, cadherins, and plexin receptors. However, a systematic investigation of their substrate specificities is lack  ...[more]

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