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Comprehensive O-GlcNAc glycoproteomics on NOTCH1 EGF repeats refined the sequons for O-GlcNAcylation and uncovered unique Lewis X epitopes in mammals

ABSTRACT: This study performed the comprehensive mass spectrometric analyses of O-GlcNAc glycans on NOTCH1 in mammalian cultured cells. The results indicated that the O-GlcNAcylation occurs only a subset of EGF repeats harboring putative O-GlcNAcylation sites, refining the sequons for extracellular O-GlcNAcylation in mammals. Moreover, novel structures with fucosylated O-GlcNAc glycans were identified and the similar structure was detected on O-fucose glycans, extending the view of structural diversity of functional Notch O-glycans.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Tetsuya Okajima

PROVIDER: PXD022387 | JPOST Repository | Sat Nov 06 00:00:00 GMT 2021

REPOSITORIES: jPOST

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			Action	DRS
	Fig1B_Trp_%231.raw	Raw
	Fig1B_Trp_%232.raw	Raw
	Fig1B_Trp_%233.raw	Raw
	Fig2A_%231.raw	Raw
	Fig2A_%232.raw	Raw

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Comprehensive O-GlcNAc glycoproteomics on NOTCH1 EGF repeats refined the sequons for O-GlcNAcylation and uncovered unique Lewis X epitopes in mammals

Project description:This study performed the comprehensive mass spectrometric analyses of O-GlcNAc glycans on NOTCH1 in mammalian cultured cells. The results indicated that the O-GlcNAcylation occurs only a subset of EGF repeats harboring putative O-GlcNAcylation sites, refining the sequons for extracellular O-GlcNAcylation in mammals. Moreover, novel structures with fucosylated O-GlcNAc glycans were identified and the similar structure was detected on O-fucose glycans, extending the view of structural diversity of functional Notch O-glycans.

2021-11-06 | PXD022388 | JPOST Repository

Comprehensive O-GlcNAc glycoproteomics on NOTCH1 EGF repeats refined the sequons for O-GlcNAcylation and uncovered unique Lewis X epitopes in mammals

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Comprehensive O-GlcNAc glycoproteomics on NOTCH1 EGF repeats refined sequons for O-GlcNAcylation and uncovered unique Lewis X epitopes in mammals

Project description:The O-GlcNAc modification of Notch receptors regulates Notch ligand interactions in a manner distinct from other forms of O-glycans on epidermal growth factor-like (EGF) repeats of Notch receptors. Although many proteins, besides Notch receptors, are expected to be O-GlcNAcylated by EGF domain-specific O-GlcNAc transferase (EOGT), only a small number of proteins have been reported to be modified in vivo, and elongated O-GlcNAc glycans have not been extensively explored. To extend our view of the specificity and variety of the glycan modification, we conducted a comprehensive analysis of O-GlcNAc glycans on NOTCH1 in mammals. Mass spectrometric analysis of NOTCH1 fragments expressed in HEK293T cells revealed that several EGF domains with putative O-GlcNAcylation sites were hardly modified with O-GlcNAc. Although amino acid residues before the modification site are preferentially occupied with aromatic residues, Phe and Tyr are preferrable to Trp for the apparent modification with O-GlcNAc. Furthermore, a minor form of fucosylated O-GlcNAc glycans was detected in a subset of EGF domains. Fucosylation of O-GlcNAc glycans was enhanced by FUT1, FUT2, or FUT9 expression. The FUT9-dependent Lewis X epitope was confirmed by immunoblotting using an anti-Lewis X antibody. As expected from the similarity in the glycan structures, the Lexis X antigen was detected on O-fucose glycans. Notably, the Lewis X structure on O-glycans was identified in endogenous NOTCH1 isolated from MCF7 cells. Our results refined the putative consensus sequence for the EOGT-dependent extracellular O-GlcNAc modification in mammals and revealed the structural diversity of functional Notch O-glycans.

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Comprehensive O-GlcNAc glycoproteomics on NOTCH1 EGF repeats refined sequons for O-GlcNAcylation and uncovered unique Lewis X epitopes in mammals

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Project description:O-linked-N-acetylglucosamine (O-GlcNAc) has emerged as a critical regulator of diverse cellular processes, but its role in embryonic stem cells (ESCs) and pluripotency has not been investigated. Here we show that O-GlcNAcylation directly regulates core components of the pluripotency network. Blocking O-GlcNAcylation disrupts ESC self-renewal and reprogramming of somatic cells to induced pluripotent stem cells. The core reprogramming factors Oct4 and Sox2 are O-GlcNAcylated in ESCs, but the O-GlcNAc modification is rapidly removed upon differentiation. O-GlcNAc modification of Threonine 228 in Oct4 regulates Oct4 transcriptional activity and is important for inducing many pluripotency related genes, including Klf2, Klf5, Nr5a2, Tbx3 and Tcl1. A T228A point mutation that eliminates this O-GlcNAc modification reduces the capacity of Oct4 to maintain ESC self-renewal and reprogram somatic cells. Overall, our study makes a direct connection between O-GlcNAcylation of key regulatory transcription factors and the activity of the pluripotency network. 2 of E14 stem cell, 2 of embryonic body at day 2, 2 of embryonic body at day 2 treated with streptozotocin, 1 of ZHBTc4 stem cell treated with doxicyclin, and 1 of ZHBTc4 stem cell treated with doxicyclin and streptozotocin were analysed

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