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Phoomak C, Park D, Silsirivanit A, Sawanyawisuth K, Vaeteewoottacharn K, Detarya M, Wongkham C, Lebrilla CB, Wongkham S. O-GlcNAc-induced nuclear translocation of hnRNP-K is associated with progression and metastasis of cholangiocarcinoma. Molecular oncology 2019 13(2) 30444036
Abstract:
O-GlcNAcylation is a key post-translational modification that modifies the functions of proteins. Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported. However, the specific O-GlcNAcylated proteins (OGPs) that participate in promotion of CCA progression are poorly understood. OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database. From the proteomic analysis, a total of 21 OGPs related to cancer progression were identified, of which 12 have not been previously reported. Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression. O-GlcNAcylation of hnRNP-K was further verified by anti-OGP/anti-hnRNP-K immunoprecipitations and sWGA pull-down assays. The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression. In native CCA cells, hnRNP-K was primarily localized in the nucleus; however, when O-GlcNAcylation was suppressed, hnRNP-K was retained in the cytoplasm. These data signify an association between nuclear accumulation of hnRNP-K and the migratory capabilities of CCA cells. In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients. This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
Species: Homo sapiens
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Qin K, Zhu Y, Qin W, Gao J, Shao X, Wang YL, Zhou W, Wang C, Chen X. Quantitative Profiling of Protein O-GlcNAcylation Sites by an Isotope-Tagged Cleavable Linker. ACS chemical biology 2018 13(8) 30059200
Abstract:
Large-scale quantification of protein O-linked β- N-acetylglucosamine (O-GlcNAc) modification in a site-specific manner remains a key challenge in studying O-GlcNAc biology. Herein, we developed an isotope-tagged cleavable linker (isoTCL) strategy, which enabled isotopic labeling of O-GlcNAc through bioorthogonal conjugation of affinity tags. We demonstrated the application of the isoTCL in mapping and quantification of O-GlcNAcylation sites in HeLa cells. Furthermore, we investigated the O-GlcNAcylation sensitivity to the sugar donor by quantifying the levels of modification under different concentrations of the O-GlcNAc labeling probe in a site-specific manner. In addition, we applied isoTCL to compare the O-GlcNAcylation stoichiometry levels of more than 100 modification sites between placenta samples from male and female mice and confirmed site-specifically that female placenta has a higher O-GlcNAcylation than its male counterpart. The isoTCL platform provides a powerful tool for quantitative profiling of O-GlcNAc modification.
O-GlcNAc proteins:
A0A0A6YVU8, A0A1B0GSG7, RBM47, ZN335, A2A8N0, TITIN, SBNO1, CNOT1, PHRF1, ZN462, TAGAP, D3YUK0, E9PUR0, E9PVW1, E9PWI7, E9PYB0, PARP4, E9PZS2, E9Q2C0, E9Q3G8, E9Q616, BD1L1, E9Q732, ARHG5, E9Q7N9, E9Q842, E9Q9B4, E9Q9Q2, E9QA22, E9QAE1, F6Y6L6, F8VQ29, F8VQM5, J9JI28, PDLI1, SPT5H, TAF4, ARI1A, ABLM1, KMT2D, MYPT1, ZN609, SET1A, SYNEM, PUR4, TNC18, KDM6A, DPOD2, M3K7, TPD54, SYNJ1, ZN207, SRPK2, ACK1, SYUA, MYPT2, KIF1B, HBP1, OGA, VINEX, PLIN3, MAFK, BRD4, PDLI1, KDM6A, SRPK1, N4BP1, ANR17, NCOR1, CREG1, CRTAP, MYO1A, MTR1L, CREG1, TOX4, SUN1, M3K6, PSMG1, SC24B, CNOT4, ABL1, ABL1, EGFR, LAMC1, LMNA, GLCM, GCR, HSPB1, PPBT, RLA2, ITB1, K1C18, K2C8, SAP, CATL1, LAMB1, ENPL, BGLR, NFIC, VIME, SNRPA, ROA1, ATX1L, TGAP1, GLI2, HLAC, CATB, TAU, BIP, FINC, K2C8, TPR, MSH3, ENPL, PO2F1, ATF2, GNS, ZEP1, RS2, MUC1, JUNB, ATF7, CATD, SON, SERPH, NELFE, BIP, ROA2, CBL, IF4B, APC, ARNT, MAP4, TEAD1, RXRA, RXRB, RXRG, CLIP1, AIMP1, HXA11, ELF1, NU214, MP2K2, VATA, CUX1, PBX2, MLH1, STAT3, SSRB, KI67, STT3A, RFX5, LMNA, DPOD2, PAXI, CDK8, YLPM1, NU153, RBP2, TAF6, EMD, PPT1, FXR1, ICAL, HCFC1, AGFG1, NUP98, ATX1, ATN1, PTN5, AF17, DSRAD, AMRP, ACYP2, NU107, ACOT8, S26A1, TB182, YTHD1, ASXL1, PI5PA, RIN3, MRTFB, RL37, KCNA2, RALA, STIM1, PITX1, IF4G2, SRPK2, RENBP, COG7, WNK1, SERF2, RPTN, SPSY, DAB2, RBM10, HNRPU, SPTB2, FOXK2, EWS, MEF2A, SP2, CO7A1, S30BP, NUCB1, ENL, IF4G1, K1C17, TLE3, TLE4, TOP1, SUH, CBG, ACK1, DEMA, AHNK, FOXO1, TROAP, BPTF, NFIA, ROA0, G3BP1, PABP4, ATM, PICAL, MAMD1, RIPK1, STIM1, MTMR1, CUL4B, ASPP2, KLF5, NFYC, CDK13, VEZF1, DSG2, TRI29, UBP2L, SRC8, PUM1, EPN4, RRP1B, NCOA6, DIP2A, MEF2D, NUMA1, R3HD1, KIF14, EBP, RCN1, KS6A1, RBMS2, TAF1C, NCOA2, SF01, JHD2C, MARE1, ELF2, TAB1, ZFHX3, ZYX, ADRM1, CCDC6, TAF9, STX1A, RFX7, QSER1, QRIC1, PRC2C, PBIP1, GSE1, TNR6A, CEAM5, Q3UKP4, COBL1, ARH40, SC31A, PEG3, SRBS2, Q3UU43, F91A1, ARBK2, Q497W2, Q4KL65, PHAR4, EPC2, CRTC2, BCORL, K2026, TGO1, PRC2B, TOIP1, SPG17, SHRM1, ZN362, LRIF1, RHG21, UBAP2, RBM26, RPRD2, ZN318, NCOR1, LAMA5, HCFC1, P3C2A, SAP, AP180, MAFK, SPTB2, SH3G1, ZYX, TSH3, INADL, WAPL, KAZRN, SBNO1, ARID2, DYH17, SAM9L, CDK13, LAR4B, BICRL, RHG21, HELZ, TTLL5, PANX2, PKHG2, NIPBL, LIN54, F135A, RPRD2, IF4G1, SPIC, SCYL2, NFRKB, INT1, ZN182, UGGG1, MDEAS, ZC3HE, RICTR, FIP1, CRTC3, SAS6, MCAF1, BCOR, GGYF2, NU188, CO039, UBN2, HAKAI, ASXL2, SPT6H, DDX46, KDM3B, PICAL, PRC2B, OOG2, ZIC5, NRK, POGZ, MAVS, CLAP1, EMSY, I2BP2, SRGP1, SH3R1, HUWE1, YTHD3, NU214, UBP2L, TMC5B, ZN598, TOPRS, SHAN2, Q80ZX0, ZNF18, Q810G1, BCL9L, LUZP1, PRSR1, DDX42, PALB2, P66A, GNS, LPP, TB10B, TGO1, Q8BIB6, ZN771, ZNT6, AAPK2, CNOT4, SP110, IFFO1, YTHD3, NCBP3, DEFI6, RBM14, CNOT2, CABS1, Q8C6L9, TCAL5, TAB1, SCYL2, ASPP2, PHC3, EPN2, PDLI5, I2BP1, RN135, AHNK2, NAV2, MISP, MGAP, ANKH1, PHAR4, XRN1, PELP1, Q8JZK6, Q8K0U8, AGFG1, TXD11, IL23R, ARHG6, SPART, SPICE, NUP93, CLASR, ZN786, SYNPO, FNBP4, ARFG1, ENAH, TNR6A, PHC3, SP20H, NAV1, VP37A, KMT2C, BD1L1, NUP35, STXB6, KNL1, TCAL3, MTSS1, SPART, NUP35, PUM2, STT3B, ALMS1, GEMI5, WIPF2, MAVS, UTP6, PI3R4, AMOT, P66B, STAG1, PCNP, LMO7, ATX2L, CSKI2, P66B, BBX, TITIN, HNMT, UBAP2, DCP1A, NRIF1, SMG7, RTF1, MAML1, ZN592, LAR4B, TAF4B, SHIP1, DDX17, RENT1, GPKOW, FUBP2, LPP, TTC28, PF21A, INT12, RCN3, CERS2, PDLI5, FUBP3, MY15B, ANCHR, CLP1L, Z512B, ZFR, EP400, NOL4L, RBM14, CIC, MED15, PIGS, DCR1C, SIN3A, MINT, EYA3, TEAD3, ATX2, RFC4, DHX58, ANX13, GORS2, TAB2, EPN4, ANR17, DPH2, WAC, DIDO1, YTHD1, AMRA1, TANC1, TXD12, F133B, RBM33, GPI8, Q9D2U0, ZC21B, FUND2, F162A, APMAP, Q9D809, FIP1, CNPY3, Q9DAV5, Q9DB24, ALG2, PLIN3, MYPT1, WWTR1, Q9EQC8, SALL1, RBP2, GILT, MFF, SP130, APC1, I2BPL, RBNS5, EPC1, ADNP, ZN106, TM245, CPVL, PTN23, WNK1, E41L1, ZHX3, ZN335, PKHG2, CCSE2, CQ10B, MLXIP, PKHA5, RC3H2, TAF9B, ZBT20, NCOA5, ZN532, APMAP, HYOU1, ADRM1, GIT2, BAG3, UBN1, PDLI7, DIAP3, RBM12, CARF, ETAA1, HXC10, TAB2, UGGG1, CDK12, ITSN2, CNOT2, TMEM9, DAPLE, NYAP2, KANL3, SON, LIMD1, KI21B, KI21A, PPIE, PCM1, GALK1, MRP5, SE1L1, LIMD1, TCF20, SUN2, AFF4, UBQL2, S30BP, NRBP, SIX4, TASOR, GMEB2, PARP4, NUP50, ZHX1, YETS2, HECD1, SCAF8, SRRM2, SCML2, S22AL, NCOR2, DEMA, POLH, R3HD2, ZN281, FBX7, RPGF2, IRS2, HYOU1, PRC2C, NCOR2, GMEB1, S23IP, SRPK3, Q9Z0I7, VNN1, KLK4, SE1L1, RGS6, E41L1
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Shen B, Zhang W, Shi Z, Tian F, Deng Y, Sun C, Wang G, Qin W, Qian X. A novel strategy for global mapping of O-GlcNAc proteins and peptides using selective enzymatic deglycosylation, HILIC enrichment and mass spectrometry identification. Talanta 2017 169 28411811
Abstract:
O-GlcNAcylation is a kind of dynamic O-linked glycosylation of nucleocytoplasmic and mitochondrial proteins. It serves as a major nutrient sensor to regulate numerous biological processes including transcriptional regulation, cell metabolism, cellular signaling, and protein degradation. Dysregulation of cellular O-GlcNAcylated levels contributes to the etiologies of many diseases such as diabetes, neurodegenerative disease and cancer. However, deeper insight into the biological mechanism of O-GlcNAcylation is hampered by its extremely low stoichiometry and the lack of efficient enrichment approaches for large-scale identification by mass spectrometry. Herein, we developed a novel strategy for the global identification of O-GlcNAc proteins and peptides using selective enzymatic deglycosylation, HILIC enrichment and mass spectrometry analysis. Standard O-GlcNAc peptides can be efficiently enriched even in the presence of 500-fold more abundant non-O-GlcNAc peptides and identified by mass spectrometry with a low nanogram detection sensitivity. This strategy successfully achieved the first large-scale enrichment and characterization of O-GlcNAc proteins and peptides in human urine. A total of 474 O-GlcNAc peptides corresponding to 457 O-GlcNAc proteins were identified by mass spectrometry analysis, which is at least three times more than that obtained by commonly used enrichment methods. A large number of unreported O-GlcNAc proteins related to cell cycle, biological regulation, metabolic and developmental process were found in our data. The above results demonstrated that this novel strategy is highly efficient in the global enrichment and identification of O-GlcNAc peptides. These data provide new insights into the biological function of O-GlcNAcylation in human urine, which is correlated with the physiological states and pathological changes of human body and therefore indicate the potential of this strategy for biomarker discovery from human urine.
O-GlcNAc proteins:
TX13C, ESYT2, BICL2, ODAM, SRCRL, SYTC2, Z804B, O2A25, XIRP2, NKX26, SMCO2, MFS2B, O51F1, NCF1B, BTBDB, SRRM4, D11L8, YV023, LEUTX, MEIOS, RB27B, CACB4, SOCS6, CHD1, NDC80, KIF3C, MYPT1, IPP2C, MUSK, MRP3, PA2GX, ARPC5, P2RX6, ZW10, ZN749, KCAB3, ACTN4, VEGFD, BNI3L, ZN292, PI51C, MABP1, CCG3, NOBOX, REV3L, TBL1X, NBN, KI21B, PX11A, UBP2, CAN15, ATRN, SPF30, MYO1D, SUN1, ENDD1, M4K4, CFAB, LV151, K1C14, K2C1, HSPB1, CHLE, SAP, SRPRA, GNAI3, IL6RA, VILI, AT8OS, GLI3, RNAS2, LYAG, SPTB1, PSG2, LAMP2, CSPG2, SC5A1, F261, DPEP1, EPB42, ITB6, LMNB1, NEBU, RYR1, TENX, SP100, ANX13, ADH6, GNA11, NMT1, CPSM, GBRA5, AKT2, I5P2, MYH11, HMGCL, PGM1, CDN1A, MLH1, SATT, DCC, MAGAA, MMP13, ABCG1, MP2K3, UTRO, IDHP, PSB3, RBP2, MRE11, ETV1, IRAK1, ARSD, NEK4, SPSY, COPA, SMTN, ATN1, PMS1, PMS2, ATNG, PRRX1, AF17, NXPH1, NAL12, IF4A1, STX1B, KCNJ2, HPCA, PKD1, REEP5, CAC1D, MMSA, SEMG2, ACY1, P, ZNF91, LG3BP, PDE4C, SCAP, PO4F2, NMDE1, OVGP1, ANK3, NFAC3, AKAP6, CENPR, SF3B2, TRA2A, CUL4B, ALKB1, CO9A2, FA53B, WRN, SLBP, GOGB1, ZN169, ODFP1, FRPD4, MELT, SART3, IF4H, KIF14, PLCL1, PLEC, PSG5, DLGP5, MARE2, ENOX2, CNGA2, AINX, HCDH, CSPP1, QSER1, ZN423, SPKAP, PRSR3, F214A, K2C71, GON4L, GNPTA, LEGL, PAR14, PCDP1, PLCH1, AARD, RHG29, SPIN4, FA76B, CX066, BRM1L, ODR4, SZT2, SYRM, F102B, CE162, CA195, CL060, MYOME, ARHGG, CA140, CARL1, ZMYM4, EST4A, F219B, WDR25, F90A2, LAR1B, ATG9B, ARID2, FTM, USF3, KCD16, ZNF57, K1C39, Z518A, URFB1, CV042, RTL6, CAPR2, ADAM5, ZNT6, CA094, VIP1, AGRD1, CC171, KLH24, ABRX1, PAMR1, TM14E, ITIH6, RFIP1, IGS10, WDR87, SHSA6, FGD6, RGMC, NEK10, UBP31, NOL8, MARK2, BEND5, PCAT2, EPMIP, DPH6, OLIG3, TRPM8, CC186, MYCPP, TMC7, Z804A, TAF8, RALYL, RBM23, CC190, PKHL1, GA2L3, TCAM2, STX12, KI18B, RB6I2, ARMC8, K0825, STH, RP1L1, TPH2, F217A, PLPL6, EFC13, CJ067, PSYR, TBC21, DOCK3, AGRF4, SYCE1, CADM3, CP4Z2, CLASR, ZN786, CLIP4, CBPA6, NKAP, TM156, CPSF7, EFNMT, IGS22, LMBL4, ZFP62, PHC3, DDHD1, EXPH5, NAV1, BD1L1, BPIB6, TET1, MYRIP, FBH1, O10K1, ST3L4, CHD6, DMXL2, MIPT3, ES8L3, DOT1L, NAT14, CKAP2, ARAP3, CSKI1, ATRIP, MUC16, ELYS, TITIN, LZIC, PHF3, TBCD5, K0232, PRCC, TFG, SFRP3, COR2A, ARHG2, TATD2, LENG9, FAM3D, ALKB8, CHM4C, LRC58, REPS1, PGBD4, P3IP1, CDCA5, HMCES, DMAC1, IGS21, PAWR, ITCH, M4A14, CLMN, S41A2, HSH2D, TM87B, ZN514, P12L2, C295L, CQ10A, ROBO3, WWAS2, DB118, KI20B, PHF12, SPAG5, OR2M4, HMCN1, RANB9, CCNL2, IWS1, K1C12, NPY6R, S1PR3, LYST, CDC6, EBP2, NIPS1, DDX50, FA83C, PIMRE, NDC1, MTNA, UT14A, NUP85, TDRD1, MSTRO, SETD2, OSBL8, UACA, TSG10, TB182, EGLN1, CRLD2, CSTFT, NKX24, CT191, ESF1, PIEZ2, CE066, RANB3, CSR2B, UCK1, ZN556, MLXIP, TNR6C, HMX1, EQTN, PRDM9, TLR8, HELLS, TOPRS, KIF15, RAD18, HOME2, BRWD1, TEN2, CCM2L, FGOP2, MCUB, MIC19, KCTD5, CARF, FAT2, DTL, SACS, KLHL8, CE126, WDR35, NRX2A, DNM3B, COPG2, GCP4, PARP2, TCF20, ASIC3, RABX5, STAG3, NGAP, FBX5, MKLN1, ZBT21, PKHH1, SOX13, LIMC1, EXOC7, CBPC1, TUTLB, XCT, SHOC2, RUVB2, PDE10, PRLD1, FBW1A, DLGP4, WDR37, ZBTB1, NSG2, LSM2, DOP2, C170B, SAM50, PCDBB, PCDA3, TF3C3, CCG2, BIG1, S4A4, PCLO
Species: Homo sapiens
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Lund PJ, Elias JE, Davis MM. Global Analysis of O-GlcNAc Glycoproteins in Activated Human T Cells. Journal of immunology (Baltimore, Md. : 1950) 2016 197(8) 27655845
Abstract:
T cell activation in response to Ag is largely regulated by protein posttranslational modifications. Although phosphorylation has been extensively characterized in T cells, much less is known about the glycosylation of serine/threonine residues by O-linked N-acetylglucosamine (O-GlcNAc). Given that O-GlcNAc appears to regulate cell signaling pathways and protein activity similarly to phosphorylation, we performed a comprehensive analysis of O-GlcNAc during T cell activation to address the functional importance of this modification and to identify the modified proteins. Activation of T cells through the TCR resulted in a global elevation of O-GlcNAc levels and in the absence of O-GlcNAc, IL-2 production and proliferation were compromised. T cell activation also led to changes in the relative expression of O-GlcNAc transferase (OGT) isoforms and accumulation of OGT at the immunological synapse of murine T cells. Using a glycoproteomics approach, we identified >200 O-GlcNAc proteins in human T cells. Many of the identified proteins had a functional relationship to RNA metabolism, and consistent with a connection between O-GlcNAc and RNA, inhibition of OGT impaired nascent RNA synthesis upon T cell activation. Overall, our studies provide a global analysis of O-GlcNAc dynamics during T cell activation and the first characterization, to our knowledge, of the O-GlcNAc glycoproteome in human T cells.
Species: Homo sapiens
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Nandi A, Sprung R, Barma DK, Zhao Y, Kim SC, Falck JR, Zhao Y. Global identification of O-GlcNAc-modified proteins. Analytical chemistry 2006 78(2) 16408927
Abstract:
The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins. The functions and subproteome of O-GlcNAc modification remain largely undefined. Here we report the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins. The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies. Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation. Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
Species: Homo sapiens
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