REFERENCES



Choose an author or browse all
Choose the species or browse all
Choose a criteria for sorting
 Reverse sorting
Search for a protein
Search for a single PMID
Select O-GlcNAc references filter

Click to expand (39 results)


Luo Y, Wang Y, Tian Y, Zhou H, Wen L. "Two Birds One Stone" Strategy for the Site-Specific Analysis of Core Fucosylation and O-GlcNAcylation. Journal of the American Chemical Society 2023 37340703
Abstract:
Core fucosylation and O-GlcNAcylation are the two most famous protein glycosylation modifications that regulate diverse physiological and pathological processes in living organisms. Here, a "two birds one stone" strategy has been described for the site-specific analysis of core fucosylation and O-GlcNAcylation. Taking advantage of two mutant endoglycosidases (EndoF3-D165A and EndoCC-N180H), which efficiently and specifically recognize core fucose and O-GlcNAc, glycopeptides can be labeled using a biantennary N-glycan probe bearing azido and oxazoline groups. Then, a temperature-sensitive poly(N-isopropylacrylamide) polymer functionalized with dibenzocyclooctyne was introduced to facilitate the enrichment of the labeled glycopeptides from the complex mixture. The captured glycopeptides can be further released enzymatically by wild-type endoglycosidases (EndoF3 and EndoCC) in a traceless manner for mass spectrometry (MS) analysis. The described strategy allows simultaneous profiling of core-fucosylated glycoproteome and O-GlcNAcylated glycoproteome from one complex sample by MS technology and searching the database using different variable modifications.
O-GlcNAc proteins:
LCE6A, RBM47, HFM1, SMCO3, SBNO1, ODAD3, CNOT1, RCCD1, GLTD2, AGAP5, CX049, PDLI1, TAF4, ABLM1, DVL1, HGS, SC16A, NPC1, LAMA5, TET3, IF4G3, E41L2, AKAP8, PLIN3, MAFK, OPHN1, MITF, OBSL1, ANR17, ENTP6, NCOR1, ERLN1, JERKY, MYCB2, WDHD1, CBPD, TOX4, AGFG2, SC24B, PCNT, BAG3, DDAH2, CLPT1, AACT, LMNA, FINC, FETUA, GCR, KITH, HSPB1, RPN1, RLA2, ITB1, K1C18, ENOA, CATD, TBB5, TACD2, LYAG, BIP, LAMC1, HSP7C, DMD, MPRI, SKI, GILT, GLU2B, ENPL, RSMB, PO2F1, PVR, ZEP1, DPEP1, CBPE, ATF7, SON, ATF1, ITIH2, FST, ICAL, FGF7, CD9, CBL, ITA6, PTPRB, COF1, GATA3, PSA4, PEBP1, CLIP1, ZEP2, GLPK, ELF1, CD68, GPC1, HRH1, IRS1, NU214, SRP14, NUP62, ETFB, LICH, TXLNA, STAT3, MATR3, SSRA, GATA4, MMP13, 5HT3A, NOTC1, YAP1, RFX5, FAS, CDK8, CENPF, NU153, SEPP1, EMD, BCAM, HCFC1, SPHM, ARSD, AGFG1, NUP98, PTTG, RAD, AF17, DSRAD, ITA1, IF6, STAR6, ACTB, HNRPK, H4, RL40, CXAR, GPC5, FOXK1, PGBM, SPTB2, FOXK2, IF4G1, NOTC2, TLE3, PTN12, MTG8, ZO1, LRP1, RGS1, CD47, EP300, AHNK, TROAP, BPTF, NFIA, HYAL2, LMAN2, FOXC1, MB211, OS9, TUSC3, ROCK1, ASAH1, RIPK1, ASPP2, CDK13, SCRB2, VEZF1, DSG2, UBP2L, GIT2, PUM1, RRP1B, NCOA6, MEF2D, CHD4, NUMA1, R3HD1, RCN1, RBMS2, TAF1C, SF01, JHD2C, ELF2, TAB1, HERC1, ZFHX3, ZYX, ADRM1, CCDC6, SNPC1, MA2A1, YC018, QSER1, AAK1, P3H1, GNPTA, RABL6, TB10B, LUZP6, PRC2B, WIPI1, DCA10, HP1B3, ZN362, ZEP3, ZC3HD, UBR4, RHG21, UBAP2, RPRD2, DNAI4, TASO2, RN123, PCX4, ARID2, FTM, BICRL, SCAR3, GRHL2, NIPBL, LIN54, NFRKB, ZC3HE, LCN15, CREL2, IGS10, GGYF2, NBEL2, SRCAP, K0408, UBN2, BACHL, KDM3B, PARPT, RGPD4, POGZ, MAVS, EMSY, RAI1, I2BP2, ABCAC, ZFHX4, LUZP1, FRAS1, RB6I2, AHNK2, S22A9, TEX2, MGAP, SULF2, ANKH1, SUGP1, HYCC2, MILK2, CC116, PHAR4, K319L, ASPM, RPTOR, SYNPO, GALT4, MFSD9, SLAI1, CC168, TNR6A, PHC3, VP37A, SYNE1, PLBL2, TIP, CC110, TEX47, TBC15, STT3B, SPP2B, MAGC3, DYH5, PO210, GEMI5, PIGO, F222B, F151A, LMO7, P66B, MYO3B, GBF1, NICA, TM131, ZN592, LAR4B, GSLG1, GPKOW, LPP, TTC28, PF21A, RBM33, GWL, TONSL, PDLI5, VCIP1, ZFR, EP400, CH048, CI072, NOL4L, RBM14, GBP4, CDK15, PHF12, CIC, MED15, G3ST4, FNBP1, MINT, HTF4, EYA3, ARI3A, H2A1J, GDF15, DPH2, BCL7B, TM2D3, PELO, DIDO1, TRAIP, RBM4, CLC7A, UBE2O, PEG3, SP130, BRD8, I2BPL, EPC1, ADNP, RM46, NELFA, WNK1, ZHX3, SDS3, MLXIP, RC3H2, MUC5B, TANC2, CHD8, CELR2, APMAP, PDLI7, RBM12, STAU2, GPTC2, TAB2, CDK12, PTTG3, FLRT1, CRIM1, DAPLE, IBTK, RBM27, KANL3, RERE, SE1L1, LIMD1, TCF20, DPP2, BAP29, S30BP, LCAP, BTNL2, SIX4, POMT2, INT6, MRTFB, NOTC3, ATS5, BSN, SCAF8, ANR26, SHAN2, SRRM2, CTND2, SCML2, ZN652, ZN281, STRAP, VPP2, PRC2C, NCOR2, DC1L1, STON1, S23IP
Species: Homo sapiens
Download
Jackson EG, Cutolo G, Yang B, Yarravarapu N, Burns MWN, Bineva-Todd G, Roustan C, Thoden JB, Lin-Jones HM, van Kuppevelt TH, Holden HM, Schumann B, Kohler JJ, Woo CM, Pratt MR. 4-Deoxy-4-fluoro-GalNAz (4FGalNAz) Is a Metabolic Chemical Reporter of O-GlcNAc Modifications, Highlighting the Notable Substrate Flexibility of O-GlcNAc Transferase. ACS chemical biology 2022 17(1) 34931806
Abstract:
Bio-orthogonal chemistries have revolutionized many fields. For example, metabolic chemical reporters (MCRs) of glycosylation are analogues of monosaccharides that contain a bio-orthogonal functionality, such as azides or alkynes. MCRs are metabolically incorporated into glycoproteins by living systems, and bio-orthogonal reactions can be subsequently employed to install visualization and enrichment tags. Unfortunately, most MCRs are not selective for one class of glycosylation (e.g., N-linked vs O-linked), complicating the types of information that can be gleaned. We and others have successfully created MCRs that are selective for intracellular O-GlcNAc modification by altering the structure of the MCR and thus biasing it to certain metabolic pathways and/or O-GlcNAc transferase (OGT). Here, we attempt to do the same for the core GalNAc residue of mucin O-linked glycosylation. The most widely applied MCR for mucin O-linked glycosylation, GalNAz, can be enzymatically epimerized at the 4-hydroxyl to give GlcNAz. This results in a mixture of cell-surface and O-GlcNAc labeling. We reasoned that replacing the 4-hydroxyl of GalNAz with a fluorine would lock the stereochemistry of this position in place, causing the MCR to be more selective. After synthesis, we found that 4FGalNAz labels a variety of proteins in mammalian cells and does not perturb endogenous glycosylation pathways unlike 4FGalNAc. However, through subsequent proteomic and biochemical characterization, we found that 4FGalNAz does not widely label cell-surface glycoproteins but instead is primarily a substrate for OGT. Although these results are somewhat unexpected, they once again highlight the large substrate flexibility of OGT, with interesting and important implications for intracellular protein modification by a potential range of abiotic and native monosaccharides.
Species: Homo sapiens
Download