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Hao Y, Li X, Qin K, Shi Y, He Y, Zhang C, Cheng B, Zhang X, Hu G, Liang S, Tang Q, Chen X. Chemoproteomic and Transcriptomic Analysis Reveals that O-GlcNAc Regulates Mouse Embryonic Stem Cell Fate through the Pluripotency Network. Angewandte Chemie (International ed. in English) 2023 62(17) 36852467
Abstract:
Self-renewal and differentiation of embryonic stem cells (ESCs) are influenced by protein O-linked β-N-acetylglucosamine (O-GlcNAc) modification, but the underlying mechanism remains incompletely understood. Herein, we report the identification of 979 O-GlcNAcylated proteins and 1340 modification sites in mouse ESCs (mESCs) by using a chemoproteomics method. In addition to OCT4 and SOX2, the third core pluripotency transcription factor (PTF) NANOG was found to be modified and functionally regulated by O-GlcNAc. Upon differentiation along the neuronal lineage, the O-GlcNAc stoichiometry at 123 sites of 83 proteins-several of which were PTFs-was found to decline. Transcriptomic profiling reveals 2456 differentially expressed genes responsive to OGT inhibition during differentiation, of which 901 are target genes of core PTFs. By acting on the core PTF network, suppression of O-GlcNAcylation upregulates neuron-related genes, thus contributing to mESC fate determination.
O-GlcNAc proteins:
AMRA1, SETX, SKT, BCORL, AGRIN, MGAP, ARI1A, KANL3, CHD6, PHRF1, ZCH24, EP300, KIF7, KI67, CE350, ANR11, NUMA1, TPR, MORC3, TAF4B, KMT2B, EMD, AKAP1, TCOF, DCTN1, MNT, NCOA3, ATN1, ECP3, DPOD2, CTND2, PIAS3, AF10, ACK1, GET3, DSG2, ESS2, ATX2, PDLI1, ULK1, BARD1, KDM6A, ZN106, NSD1, ZFR, HIPK1, SETB1, LAMC1, MYCN, GCR, EGR1, RC3H2, ATX1L, DERPC, K2C8, HSPB1, JUND, FGFR1, G3P, ATF2, COF1, HEXB, VIME, PO5F1, CBL, CCNB1, PO2F1, RS2, NFKB1, MAX, PABP1, NEDD1, PTN12, FMR1, ELK1, FOXK1, STAT3, SOX15, PLIN2, CBP, NEDD4, YAP1, RFX1, SOX2, LMNA, ROA1, S1PR2, ARNT, RD23A, PLTP, KMT2A, KLF16, FOXP1, TB182, GMEB2, SENP1, YTHD1, MRTFB, DOCK4, STIM1, TBX3, NCOA1, ERF, SIAE, NACAM, ATF1, WNK1, G3BP2, DNLI3, G3BP1, RLA2, GABPA, S30BP, ZEP1, ENAH, SOX13, CAPR2, APLP2, CLUS, TLE3, GATA4, MITF, CHD8, ZCH18, TANC1, CDK12, SAP25, LIN41, MLXIP, HROB, VRTN, CO039, PDLI7, SMCA4, PRC2C, MILK2, MIDN, YETS2, PBIP1, FUBP2, TFPT, SRBP2, GSE1, F117B, ZN865, WDR62, QRIC1, FOXK2, RREB1, TNR6C, DAB2P, TNR6A, RHG17, PKHA7, COBL1, FCHO2, TET1, ARMX5, GARL3, TET2, CDV3, PHAR4, C2CD3, LIN54, NPA1P, TAB3, TASO2, RESF1, NUFP2, UNKL, COBL, KDM6B, PRSR1, SMG7, RBM27, PHF12, ZDBF2, PUR4, SYNRG, UIMC1, SIN3A, NFAC2, SRC8, SKIL, ELF1, KLF4, NCOR1, KLF3, NCOA2, FOXD3, PAPOA, HCFC1, P3C2A, SIX4, ZFHX3, TOB1, AP180, GLI3, ATRX, MAFK, NPM, M3K7, DAG1, SPTB2, TAF6, TIF1B, SPT6H, SH3G1, ARI3A, TLE1, TLE4, IF4G2, MINT, ZIC3, ZYX, NUP62, PHC1, TFE3, TIF1A, SF01, DAZL, RBL1, KNL1, BCL9L, SBNO1, SLAI1, PKP4, CDK13, SH3R1, JHD2C, HECD1, ARMX2, LAR4B, RHG21, HELZ, SCAF8, UTF1, PKHG2, NIPBL, CCD66, F135A, RPRD2, WWC2, ZN532, KRBA1, TAF9B, RBM26, INT1, BCR, AHDC1, PTN23, PAPD7, KDM3A, KMT2D, CHD4, RN220, NUP98, NFRKB, GGYF2, LCOR, TEX2, PF21A, KDM3B, FNBP4, CNOT1, LARP1, RHG26, NU188, CNDD3, PICAL, SPAG5, HUWE1, SMAP2, CPEB3, MYCB2, PRC2B, PRR14, MACOI, ATX2L, CKP2L, PRC2A, MCAF1, SI1L2, KANL1, ERBIN, R3HD2, RERE, PUM2, PUM1, NU214, WNK4, TCAM1, SAS6, CAMP3, UBN2, TNC18, AGFG2, UBP2L, WNK3, ZN598, CTIP, SHAN2, NANOG, DDX42, RHG32, VGLU3, LPP, TET3, MYPT2, IF4B, CNO10, MISSL, TB10B, CARF, TGO1, ZN879, SP130, ZC3HE, ZNT6, SUN2, TNR6B, ARI5B, EMSY, BNC2, KAT6B, KMT2C, CLAP2, CNOT4, SRRM2, TOX4, GEPH, SYP2L, LARP4, KANK2, SALL4, YTHD3, TOIP2, KAT6A, ASXL2, POGZ, SREK1, TAF5, ZHX2, EPC2, SI1L1, CND2, RBM14, SUCO, CNOT2, DIDO1, SMAG1, LENG8, CDAN1, DPPA4, LRIF1, VCIP1, MB214, TAB1, SCYL2, ASPP2, LS14B, SYEP, F193A, BCOR, OGT1, SUGP1, NAV1, SYNJ1, ADNP2, RPGF2, BICRL, EP400, PHC3, VP37A, EPN2, P66A, PDLI5, ELYS, ZBT20, ANLN, AGFG1, MATR3, CASC3, I2BPL, PO121, ALMS1, SF3A1, GRHL2, ATF7, CACL1, DC1L1, MTSS1, SPART, TDIF2, HBP1, NUP58, RFIP5, BRD8, WIPI1, CDK8, CS047, ATX7, NUP35, LUZP1, RPAP2, NDC1, MAVS, AMOT, CSKI2, P66B, TAF9, IPO4, ZCH14, UBAP2, NCOA5, FUBP1, RBM47, AJUBA, VPS36, DCP1A, EGLN2, YTHD2, SRGP2, GRHL1, BCL7B, P4R3B, PLRG1, CIC, WAC, TRPS1, MED1, ACATN, NRBP, RP25L, NONO, TAB2, RBM10, EPN4, DDAH2, NOG2, ZN281, HGS, NASP, ARIP4, ANR17, ZN318, TRI33, MZT2, ZWINT, ECD, YIF1B, ROA0, DHRS7, TPD54, SSBP3, PSRC1, SARNP, BCL9, SP2, NOP56, SH24A, FIP1, PLIN3, MYPT1, KC1D, TCF20, TOR3A, SALL1, ZN704, RBP2, UBE4B, TBX20, AFF4, RBCC1, 4ET, PALLD, ELF2, TSSC4, NUDT3, HAKAI, ADRM1, NCOA6, FANCA, GIT2, BAG3, TOB2, ZN207, SON, TBL1X, PLEC, MACF1, GOGA5, QKI, GAB1, DMRT1, YLPM1, PCM1, RHG07, TAF7, FOXO1, ADA23, AKA12, UXT, MAN1, NCOR2, AKT3, COR1B, TNIP1, GANP, DEMA, CARM1, RGAP1, ITSN2, ZO2, KLF5, ADNP, ARI3B, BCL3, SE1L1, E41L1, ZN292
Species: Mus musculus
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Shu XE, Mao Y, Jia L, Qian SB. Dynamic eIF3a O-GlcNAcylation controls translation reinitiation during nutrient stress. Nature chemical biology 2022 18(2) 34887587
Abstract:
In eukaryotic cells, many messenger RNAs (mRNAs) possess upstream open reading frames (uORFs) in addition to the main coding region. After uORF translation, the ribosome could either recycle at the stop codon or resume scanning for downstream start codons in a process known as reinitiation. Accumulating evidence suggests that some initiation factors, including eukaryotic initiation factor 3 (eIF3), linger on the early elongating ribosome, forming an eIF3-80S complex. Very little is known about how eIF3 is carried along with the 80S during elongation and whether the eIF3-80S association is subject to regulation. Here, we report that eIF3a undergoes dynamic O-linked N-acetylglucosamine (O-GlcNAc) modification in response to nutrient starvation. Stress-induced de-O-GlcNAcylation promotes eIF3 retention on the elongating ribosome and facilitates activating transcription factor 4 (ATF4) reinitiation. Eliminating the modification site from eIF3a via CRISPR genome editing induces ATF4 reinitiation even under the nutrient-rich condition. Our findings illustrate a mechanism in balancing ribosome recycling and reinitiation, thereby linking the nutrient stress response and translational reprogramming.
O-GlcNAc proteins:
A0A075B5P4, A0A087WNV1, A0A087WPT1, A0A087WQF8, A0A087WS88, A0A0A0MQM6, A0A0A6YVP0, A0A0A6YY72, A0A0B4J1E2, A0A0G2JFJ6, A0A0G2JFN8, A0A0G2JFY0, A0A0G2JG10, A0A0G2JG59, A0A0G2JG60, A0A0G2JG65, A0A0G2JGL8, A0A0H2UH17, A0A0J9YTU3, A0A0J9YUT8, A0A0J9YUY8, A0A0N4SV00, A0A0N4SV32, A0A0N4SW94, A0A0N5E9G7, A0A0R4J060, A0A0R4J169, A0A0R4J1E3, A0A0R4J1Y4, A0A0R4J260, A1BN54, A1L341, A1L3S7, A2A485, A2A513, A2A5N3, A2A8V8, A2AGK3, LZTS3, A2AM70, A2AMY5, A2APQ6, A2AS44, A2AVJ7, A2AWT6, A2BGG7, KANL3, K1C28, A6X8Z3, A8Y5K6, B0V2N8, B1AU25, TBD2A, THOC2, TPC11, PLXB2, RBM25, B7FAU9, B7ZWM8, B8JK33, B9EHJ3, D3YTT9, D3YUW7, D3YV30, D3YV43, D3YVH4, D3YX49, D3YX64, D3YX85, SAFB1, D3YYT0, D3YZ62, D3YZL1, D3YZT4, D3Z1X3, D3Z2H7, D3Z3E8, D3Z4B0, CCD78, D3Z6N3, CILP2, D6RCG1, E0CY31, E0CYH0, E9PUA5, E9PUJ2, E9PUX0, GCN1, E9PVC6, E9PVG8, KI67, E9PW24, E9PYF4, SET1A, E9PYI8, E9PZW0, E9Q066, E9Q0F0, E9Q0M9, E9Q0U7, E9Q0Y4, E9Q133, E9Q166, E9Q175, E9Q1Z0, E9Q2X6, E9Q3G8, NOLC1, E9Q5F6, E9Q616, MYO1E, E9Q6A9, E9Q6M7, E9Q6T8, E9Q8F0, E9Q9C7, E9Q9H2, E9QA74, E9QAT0, E9QKG6, E9QLM4, E9QN31, E9QNH6, E9QNN1, E9QPE7, E9QPI5, F2Z480, F6S6G6, F6T0G2, F6TFN2, F6TW20, F6WTC8, F6XWD4, F6YRW4, F6YUI5, F7B296, F7C312, FARP1, F8VPX1, F8VQ29, F8WHR6, G3UWP5, G3UWZ0, G3UX48, G3UYD0, G3UYG6, G3UYW3, G3UYZ0, G3X8P9, G3X8Q0, G3X956, SI1L3, G5E839, G5E846, G5E866, G5E879, G5E8C3, G5E8J8, G5E8N3, G5E8T6, H3BJU7, H3BKF6, H3BKM0, H3BKN0, H3BKT5, H3BL49, J3QMC5, J3QNW0, CAN2, ATN1, SRSF5, IMA3, PININ, EIF3D, ATX2, E41L2, UGDH, SP3, IF2B1, ZFR, HIPK1, IGKC, IGHG1, HBA, K2C1, TBA1B, ALBU, HS90A, NUCL, ATX1L, EF1A1, H2B1F, CO1A1, HS90B, TCPA, GELS, HS71L, AP2A2, K1C19, BIP, VIME, MFGM, EIF3A, MCM3, MOES, CTNA1, U2AF2, PDIA3, GRN, PABP1, FKBP4, KIF4, TSP1, GRP75, TKT, BCL6, FOXK1, H14, NEDD4, LMNA, MCM5, K2C6A, IMA1, KPYM, DDX6, ACTN4, EF2, ASXL1, ACTB, ABCE1, RRAS2, H4, HSP7C, CH60, TBA1A, TBB4B, H31, IMB1, TCPB, TCPE, TCPZ, WNK1, H32, MPRIP, G3BP1, TBB5, HNRL2, TOP2A, UBA1, PLAK, IF2P, EPS8, LRIQ1, ZCH18, LMTD2, FA83H, CDCA2, CYTSA, SPP2B, Q3TJ56, K22E, FUBP2, Q3U6F1, Q3U8S1, FOXK2, PUF60, Q3UID0, Q3UJB0, Q3UNN4, SFSWA, K22O, CFA74, Q3UYN2, LRRF1, ESF1, KIF22, Q3V3Y9, Q45VK5, Q4FJZ2, Q4KL80, Q4TU83, PDS5B, DDX17, LRC47, Q52KR6, TR150, NEXMI, JCAD, NUFP2, PRSR1, RBM27, PHF12, UTP18, LC7L3, Q5SUT0, TSR1, MYO1D, Q5U4C5, SIN3A, SRC8, MYL6, STIP1, CAPR1, IMA5, LAP2A, HCFC1, K1C15, SMRD1, FXR1, DDX5, HS71A, SERA, KINH, MYH10, SIN3B, DDX3X, TIF1B, NUP62, K1C12, SQSTM, TOP2B, Q68EM3, CLH1, CDC5L, F120A, CNDG2, NOP58, SCAF8, K1C42, K2C1B, SR140, ZC11A, ABCF1, RRP12, Q6P5B5, UGGG1, XPO1, KIF11, FHOD1, LPPRC, NUP98, Q6PGF5, NEB2, DAPLE, UBE2O, LARP1, NU188, WDR43, 2AAA, Q792Z1, PICAL, UHRF2, MBB1A, Q7TQE2, NU214, WNK4, KIRR1, UBP2L, FLNB, WNK3, Q80ZX0, LPP, ACTBL, P4HTM, MYPT2, HTSF1, IF4B, NU107, WDR3, NOC4L, CE128, NUP93, SUN2, RCC2, EMSY, SYLC, CKAP4, SRRM2, NUP54, PWP2, SYIC, RL1D1, MAP1S, TTC34, SI1L1, RBM14, Q8C872, DIDO1, ATAD2, NUP88, Q8CFQ9, SMC2, UACA, SYEP, TCRG1, OGT1, CCAR1, SLTM, BICRL, P66A, COPA, HMCS1, Q8JZN2, EIF3B, BCLF1, PHLB2, NAT10, ANLN, SDHA, LS14A, MATR3, DDX18, PO121, EIF3L, HNRPL, NU133, EIF3C, ZC3HA, TDIF2, NUP58, CD109, LUZP1, UTP6, MYH9, UHRF1, VIGLN, CCAR2, CUL7, K2C79, Q8VGW3, DHX36, SFPQ, ACLY, DDX1, U3IP2, SYYC, RPN1, YTHD2, BMP2K, SNX18, SMCA5, Q921K2, SF3B3, DDX27, Q921S6, SMTN, PP6R3, K2C5, DEN2B, NXF1, NONO, ACON, NMD3, RTCB, CT2NL, HSP7E, NU155, IF2B3, Q9CPN9, SMC1A, SMC3, CXXC1, GARS, CEP72, SC23B, Q9D6D0, NOP56, FIP1, SPB1, MYPT1, NVL, EIF3F, RAI14, CPSF1, PESC, VPS35, LIMA1, DKC1, PALLD, NUP50, DDX21, FLII, YBOX3, IQGA1, Q9QUK9, CAF1A, K1C17, MAGD1, MTA2, PR40A, MYO1C, COR1C, E41L3, EHD1, WDR46, ZO2, NU160, ADNP, SYVC, Q9Z1R9, BAZ1B, K1C16, SNUT1, S4R2A9, S4R2J9, V9GX87
Species: Mus musculus
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Huynh VN, Wang S, Ouyang X, Wani WY, Johnson MS, Chacko BK, Jegga AG, Qian WJ, Chatham JC, Darley-Usmar VM, Zhang J. Defining the Dynamic Regulation of O-GlcNAc Proteome in the Mouse Cortex---the O-GlcNAcylation of Synaptic and Trafficking Proteins Related to Neurodegenerative Diseases. Frontiers in aging 2021 2 35822049
Abstract:
O-linked conjugation of ß-N-acetyl-glucosamine (O-GlcNAc) to serine and threonine residues is a post-translational modification process that senses nutrient availability and cellular stress and regulates diverse biological processes that are involved in neurodegenerative diseases and provide potential targets for therapeutics development. However, very little is known of the networks involved in the brain that are responsive to changes in the O-GlcNAc proteome. Pharmacological increase of protein O-GlcNAcylation by Thiamet G (TG) has been shown to decrease tau phosphorylation and neurotoxicity, and proposed as a therapy in Alzheimer's disease (AD). However, acute TG exposure impairs learning and memory, and protein O-GlcNAcylation is increased in the aging rat brain and in Parkinson's disease (PD) brains. To define the cortical O-GlcNAc proteome that responds to TG, we injected young adult mice with either saline or TG and performed mass spectrometry analysis for detection of O-GlcNAcylated peptides. This approach identified 506 unique peptides corresponding to 278 proteins that are O-GlcNAcylated. Of the 506 unique peptides, 85 peptides are elevated by > 1.5 fold in O-GlcNAcylation levels in response to TG. Using pathway analyses, we found TG-dependent enrichment of O-GlcNAcylated synaptic proteins, trafficking, Notch/Wnt signaling, HDAC signaling, and circadian clock proteins. Significant changes in the O-GlcNAcylation of DNAJC6/AUXI, and PICALM, proteins that are risk factors for PD and/or AD respectively, were detected. We compared our study with two key prior O-GlcNAc proteome studies using mouse cerebral tissue and human AD brains. Among those identified to be increased by TG, 15 are also identified to be increased in human AD brains compared to control, including those involved in cytoskeleton, autophagy, chromatin organization and mitochondrial dysfunction. These studies provide insights regarding neurodegenerative diseases therapeutic targets.
O-GlcNAc proteins:
TANC2, AMRA1, CAMP1, SKT, AGRIN, KANL3, TTLL3, NHSL2, CTTB2, CCDC6, SHAN1, SYGP1, DPYL2, STXB1, CLOCK, NOTC2, VIAAT, CTND2, TPD53, REPS1, NLK, ACK1, SYUA, ATX2, PDLI1, ZFR, HCN1, BSN, TOM1, SYN1, GCR, EGR1, NFL, NFM, ATX1L, DERPC, KCC2A, CNTN1, HSPB1, MAP1B, G3P, ATF2, MTAP2, RS2, FOXK1, STAT3, AINX, EPB41, RFX1, LMNA, INPP, VATA, DVL1, CNBP, ATX1, NCAN, GOGA3, PTPA, GCP3, TB182, GMEB2, YTHD1, PI5PA, MRTFB, LIPA3, NACAM, TNIK, WNK1, NPTN, NEO1, S30BP, ZEP1, APOC2, EMAL1, RELCH, PRC2C, YETS2, FUBP2, QRIC1, LIMC1, DAB2P, ZEP2, AAK1, TNR6A, FCHO2, DRC1, SRBS2, GRM5, PACS2, OXR1, PHAR4, LIN54, MLIP, UNKL, SMG7, RBM27, CYFP2, SYNRG, SRC8, SKIL, NCOR1, LAMA5, HCFC1, P3C2A, SAP, APC, TOB1, AP180, FXR1, HS71A, LASP1, MAFK, M3K7, TAF6, ASPP1, SRBS1, DBNL, SH3G1, TLE4, IF4G2, MINT, ZYX, NUP62, OMGP, TFE3, SYN2, TBR1, RBL2, SBNO1, SLAI1, PKP4, SH3R1, JHD2C, ABLM3, ARMX2, LAR4B, HELZ, S23IP, RBM26, BCR, AHDC1, PAPD7, MFF, KMT2D, ERC2, NFRKB, WDFY3, GGYF2, TEX2, CNOT1, IF2A, PICAL, PLPR3, PRC2B, C2CD5, TPPP, ATX2L, MAP6, NAV3, AUXI, RIMB2, AVL9, NU214, AP4E1, UBP2L, C2C2L, IF4G3, ZN598, SHAN2, LPP, MYPT2, PHIPL, TB10B, CCD40, ZC3HE, DLGP2, ZC21A, BAIP2, EMSY, CLAP2, LIPA2, SRRM2, PAMR1, GEPH, YTHD3, POGZ, EPC2, SI1L1, RBM14, HYCC2, ANK2, CDAN1, SYNPO, VCIP1, TAB1, MEF2C, F193A, OGT1, EP400, EPN2, P66A, PDLI5, GTPBA, ZBT20, RTN1, BRD3, AGFG1, ABLM1, MRTFA, DC1L1, SPART, RFIP5, NUP35, WASF1, SC6A8, SGIP1, AGAP3, P66B, TAF9, WDR13, LRP5, UBAP2, BASP1, DCP1A, SYUB, TRFE, TRIM7, CIC, S12A6, GORS2, TAB2, EPN4, RNF34, ANR17, NECP1, FLIP1, ROA0, RBM33, TPD54, ODO2, DLGP1, FIP1, TM263, PLIN3, LNEBL, KC1D, NBEA, INP4A, RIMS2, RBP2, RTN3, NUDT3, ATR, ADRM1, FMN2, NCOA6, SON, ULK2, ADDA, MAGD1, MAP1A, GRM3, PCLO, GAB1, FBX6, NPAS3, GUAD, NCOR2, ATRN, NFAT5, DEMA, E41L3, SLIT3, CARM1, DYR1B, MECP2, E41L1, HDAC6
Species: Mus musculus
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Wu JL, Chiang MF, Hsu PH, Tsai DY, Hung KH, Wang YH, Angata T, Lin KI. O-GlcNAcylation is required for B cell homeostasis and antibody responses. Nature communications 2017 8(1) 29187734
Abstract:
O-linked N-acetylglucosamine (O-GlcNAc) transferase (Ogt) catalyzes O-GlcNAc modification. O-GlcNAcylation is increased after cross-linking of the B-cell receptor (BCR), but the physiological function of this reaction is unknown. Here we show that lack of Ogt in B-cell development not only causes severe defects in the activation of BCR signaling, but also perturbs B-cell homeostasis by enhancing apoptosis of mature B cells, partly as a result of impaired response to B-cell activating factor. O-GlcNAcylation of Lyn at serine 19 is crucial for efficient Lyn activation and Syk interaction in BCR-mediated B-cell activation and expansion. Ogt deficiency in germinal center (GC) B cells also results in enhanced apoptosis of GC B cells and memory B cells in an immune response, consequently causing a reduction of antibody levels. Together, these results demonstrate that B cells rely on O-GlcNAcylation to maintain homeostasis, transduce BCR-mediated activation signals and activate humoral immunity.
O-GlcNAc proteins:
FAIM3, BLTP1, BCORL, M3K15, KANL3, EXC6B, PLHD1, CTTB2, MYO1E, SCLT1, TAF4B, TCOF, FLOT1, OXLA, HDAC1, SYPL1, SEM4D, MA2B1, PPE2, PLD3, DPOD2, NOCT, HNRH1, API5, DFFA, MMP8, DPM1, EIF3D, ESS2, CTNL1, VTI1B, S28A2, FA5, CO4B, IGKC, LAC1, IGHA, IGHDM, HA11, LAMC1, TBA1B, LDHA, HVM51, SPTA1, ZFP1, EGR1, ENPL, RPB1, ITB1, ENV1, 4F2, HS90B, HA2B, HB2A, CD44, BLK, CN37, LAMP2, ZFP37, PTBP1, HB2I, BASI, FAS, EVI2A, MDR1A, BGAL, ITAL, LYN, TLN1, MOES, U2AF2, MAP4, GNA13, RL3, CATG, DPP4, PTN6, HEXA, NKTR, HMGB2, SUH, CEAM1, GTR3, DRG1, RAB5C, CD22, FMR1, VGFR1, GRP75, CAP1, ECI1, FOXK1, STAT1, NKX25, TCPQ, H11, H13, IL12B, CAPZB, RL5, VDR, RET3, ADCY7, VA0D1, AAAT, IMA1, STOM, FUS, NICA, RU2A, EF2, AAAS, RUVB1, ABCE1, DCAF7, 1433G, ACTA, RS6, VATB2, RL23, RL8, PP2BA, RACK1, TBB4B, M4K1, ITPR3, SURF6, ELAV1, EVL, H2B1A, AT8A1, TCPH, TCPB, NXN, TBB5, HNRL2, CREB1, PLAK, 3MG, CO6A1, LG3BP, COE1, CNN2, NSUN2, HMHA1, SNUT2, SMCA4, TPC10, TGRM2, I20L2, LMF1, PUF60, ZSWM8, PRRC1, SC31A, CPZIP, ITAD, ULK4, ITA1, DYHC2, LIN54, JKIP3, GRHL3, MYO1G, SIN3A, IRAG2, SAMH1, KHDR1, LY75, RASA3, NPT2A, CAPR1, ARHG2, PML, IMA5, LAP2B, PRP4B, M4K2, TS101, PLSL, CTNA2, VSX2, CD37, SERA, PCBP2, TIF1B, COCH, NUP62, RALY, UT14A, ARG39, CLH1, ATS16, F120A, NOP58, TEDC2, U520, RRP12, SMHD1, ANO6, TTBK1, CHD4, SARM1, NUP98, RASL2, TNKS1, AT1A2, NFRKB, DDX55, DNA2, H2B1C, CMYA5, GIMA8, CYFP1, SPAG5, HNRPQ, RPF1, MBB1A, PRC2A, ADCY2, MOGS, SDA1, FA98B, WIPI2, TRRAP, XYLT1, WDR82, GNS, ERLN2, S38A9, WASF2, S2512, NIM1, TBL1R, ZN526, CARF, HES7, UNC80, RBGPR, ECHA, ELMO1, ATOSB, KMT2C, FLNA, TPC2, RBBP5, POGZ, DOC10, SYFA, SMKZ, COR2A, RBM14, DOCK2, CASP9, RAE1L, NUP88, RPB2, UACA, SYEP, P66A, VPS50, COPA, VWF, TXTP, ZN536, LMBD1, R4RL1, C2D1A, URP2, STX5, GT251, SDHA, PO121, ABLM1, COL12, ALAT1, RORB, PDLI2, ERO1B, CD177, PSPC1, NUP58, STAB2, LRC8C, COX18, MAVS, PLBL1, UN93B, EVI2B, MYH9, ESIP1, VIGLN, PSMD2, HNRL1, CCAR2, SP7, RECQ5, SFXN3, IF4A3, RINI, DDX1, UBAP2, S15A4, DNJC9, MASP2, UXS1, CSCL1, BMP2K, CYRIB, SYDC, C1TC, GLYR1, PDIA6, CIC, S12A6, ATAD3, MYO5A, MCLN1, ABEC3, STML2, SFXN1, PRP19, TARA, MCRS1, RTCB, NDUS5, S12A9, SF3B1, ANR17, NU155, TR34A, BAP1, PRP8, NUDC2, TSN31, RN138, RTRAF, RU2B, YETS4, M2OM, MIC19, SNX2, DDX28, CXXC1, RUSD4, ILF2, CHTOP, LUC7L, DIM1, MCES, SEC13, SP2, NOP56, U2AF1, EF1G, MCEM1, EVPL, PRP4, CMTR1, WWP2, DHB11, PESC, TLR9, IRX6, KRT81, RBP2, AFF4, KAT2B, STK3, NUP50, DDX21, ACINU, SIGIR, ZN207, SLAF1, SON, H2AY, MTA2, SAE1, MYO1C, RUVB2, TRPV2, PFKAP, ARC1B, ASAH1, VAPA, EHD1, IF2G, CLIC1, HNRPF
Species: Mus musculus
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Morris M, Knudsen GM, Maeda S, Trinidad JC, Ioanoviciu A, Burlingame AL, Mucke L. Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice. Nature neuroscience 2015 18(8) 26192747
Abstract:
The microtubule-associated protein tau has been implicated in the pathogenesis of Alzheimer's disease (AD) and other neurodegenerative disorders. Reducing tau levels ameliorates AD-related synaptic, network, and behavioral abnormalities in transgenic mice expressing human amyloid precursor protein (hAPP). We used mass spectrometry to characterize the post-translational modification of endogenous tau isolated from wild-type and hAPP mice. We identified seven types of tau modifications at 63 sites in wild-type mice. Wild-type and hAPP mice had similar modifications, supporting the hypothesis that neuronal dysfunction in hAPP mice is enabled by physiological forms of tau. Our findings provide clear evidence for acetylation and ubiquitination of the same lysine residues; some sites were also targeted by lysine methylation. Our findings refute the hypothesis of extensive O-linked N-acetylglucosamine (O-GlcNAc) modification of endogenous tau. The complex post-translational modification of physiological tau suggests that tau is regulated by diverse mechanisms.
O-GlcNAc proteins:
KANL3, PTGDS, CTND2, RNF13, SYUA, CRIPT, BSN, THY1, CATB, TAU, AT1B2, CATD, STMN1, TB182, NACAM, WNK1, SHPS1, NOTC1, S30BP, MA6D1, PRC2C, MAST3, F117B, FOXK2, CDV3, SAP, PGCB, AP180, SRBS1, MINT, OMGP, WIPF2, PF21A, TPPP, MAP6, T106B, MAST4, LPP, C99L2, ZC21A, ENPP4, SHSA7, SYNPO, PDLI5, DIAC, LUZP1, ZFN2B, LRP1, SARNP, TM263, CRIP2, PPR1A, NUDT3, NCOA6, PCS1N, PCLO, ASAH1, APCL, MECP2
Species: Mus musculus
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Myers SA, Panning B, Burlingame AL. Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells. Proceedings of the National Academy of Sciences of the United States of America 2011 108(23) 21606357
Abstract:
The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription. The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development. To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs). Here, we unambiguously identify over 60 nuclear proteins as O-GlcNAcylated, several of which are crucial for mouse ESC cell maintenance. Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc. Together, these results provide insight into how OGT may regulate transcription in early development, possibly by modifying proteins important to maintain the ESC transcriptional repertoire.
O-GlcNAc proteins:
A2A653, A2A654, KANL3, D0VLQ4, E9QAP7, PRDX6, MAFK, ZFR, MYB, EGR1, SOX2, EBP, S30BP, TLE4, CDK12, ZFHX3, Q2TBA4, YETS2, Q3TWV0, TNR6A, Q3UY82, RESF1, SIN3A, NCOR1, TAF6, MINT, SBNO1, CDK13, JHD2C, RPRD2, NUP98, NFRKB, PF21A, KDM3B, NU188, MCAF1, NU214, Q80WR0, SP130, EMSY, SALL4, POGZ, RBM14, CNOT2, DIDO1, EP400, PHC3, AGFG1, NUP35, P66B, MED15, ZN281, ZN318, TRI33, LMAN1, SP2, PIFO, TCF20, RBP2, ELF2, YLPM1, NCOR2
Species: Homo sapiens, Mus musculus
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