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Liu X, Cai YD, Hou C, Liu X, Luo Y, Mendiola AJP, Xu X, Luo Y, Zheng H, Zhao C, Chen CH, Zhang Y, Xiang YK, Ma J, Chiu JC. O-GlcNAcylation of nuclear proteins in the mouse liver exhibit daily oscillations that are influenced by meal timing. PLoS biology 2025 23(9) 40997131
Abstract:
The liver circadian clock and hepatic transcriptome are highly responsive to metabolic signals generated from feeding-fasting rhythm. Previous studies have identified a number of nutrient-sensitive signaling pathways that could interpret metabolic input to regulate rhythmic hepatic biology. Here, we investigated the role of O-GlcNAcylation, a nutrient-sensitive post-translational modification (PTM) in mediating metabolic regulation of rhythmic biology in the liver. We observe daily oscillation of global nuclear protein O-GlcNAcylation in the liver of mice subjected to night-restricted feeding (NRF) using label-free global O-GlcNAc proteomics. Additional site-specific O-GlcNAc analysis by tandem mass tag mass spectrometry further supports temporal differences in O-GlcNAcylation by revealing day-night differences. Proteins involved in gene expression are enriched among rhythmically O-GlcNAcylated proteins, suggesting rhythmic O-GlcNAcylation may directly regulate the hepatic transcriptome. We show that rhythmic O-GlcNAcylation can also indirectly modulate nuclear proteins by interacting with phosphorylation. Several proteins harboring O-GlcNAcylation-phosphorylation interplay motif exhibit rhythmic O-GlcNAcylation and phosphorylation. Specifically, we show that O-GlcNAcylation occurs at a phospho-degron of a key circadian transcriptional activator, circadian locomotor output cycles kaput (CLOCK), thus regulating its stability and transcriptional output. Finally, we report that day-restricted feeding (DRF) in the nocturnal mouse significantly alters O-GlcNAcylation pattern. Whereas global O-GlcNAcylation analysis indicates dampening of global O-GlcNAcylation rhythm in mice fed under DRF, site-specific analysis reveals differential responses of O-GlcNAc sites when timing of food intake is altered. Notably, a substantial number of O-GlcNAcylation sites exhibit inverted day-night profiles when mice are subjected to DRF. This suggests the dysregulation of daily nuclear protein O-GlcNAcylation rhythm may contribute to the disruption in liver transcriptome previously observed in DRF condition. In summary, our results provide new mechanistic insights into metabolic regulation of hepatic transcriptional regulators via interplay between O-GlcNAcylation and phosphorylation and shed light on the deleterious effects of improper mealtimes.
O-GlcNAc proteins:
A0A075B680, A0A087WQ44, A0A087WSN6, A0A0A6YVV8, A0A0B6VMB2, A0A0F7QZE4, A0A0G2JGY6, A0A0R4J092, A0A0U1RNL9, A0A1I7Q4G8, A0A1N9PTV1, A0A1Y7VP67, A0A286YCY7, A2A654, ZMYM4, TM201, MED14, A2ADB1, A2AJ72, S35D1, BCORL, A2AQR4, A2ATN3, MGAP, KANL3, PHRF1, B1AR09, B1ASA5, B2RQG2, B2RR24, B2RT41, B2RUQ2, EP300, RBM25, B7ZNL9, D3YWX2, D3Z0K6, D3Z2U7, E9PUF4, E9PUH7, FIBA, E9PV38, SET1A, PARP4, PRR12, E9Q1A5, E9Q1M6, ICE1, E9Q3L4, ANR11, ARI1B, SETD2, YTDC1, ZC3HD, ARID2, E9Q7G1, E9Q9V3, E9Q9Y2, E9QAN9, E9QAP7, E9QKL0, E9QMD3, E9QNA7, F6R9G0, F6T8X6, BICRA, G3UVU2, G3X8Q1, G3X928, G3X961, G3X972, G3X9Q0, PCF11, G5E896, H9KV00, ERR1, GTPB1, HNF6, CLOCK, GLU2B, ATN1, IMA3, KLF12, CALU, AF10, ZN143, SP3, KDM6A, ZN106, ZFR, CCNK, PIAS1, LGMN, SP1, IGHG3, CFAH, EGR1, ITB1, ATX1L, CATB, ITPR1, B4GT1, HNF1A, PGH1, A1AT2, NFYA, PO2F1, 3BHS3, HNF1B, CEBPB, CELF1, RXRA, VTNC, NKTR, SUH, ANT3, G6PC1, FOXA1, FOXK1, STAT3, CBP, FKBP2, FOSL2, RFX1, LMNA, STS, MAT1, PON1, CEBPA, ATX1, RD23B, KMT2A, FUS, PAXB1, LMA2L, MRTFB, SUMO2, PP1B, RS11, SMD3, NFYB, SUMO1, ZHX1, TIAR, TBX3, NFYC, ATF1, ERG, NFIB, RBBP6, GABPA, CREB1, S30BP, NFIA, ZEP1, SPA3M, PPA5, CLUS, GATA4, CHD8, CDK12, Q3T9J2, KHDC4, Q3TGN5, PRC2C, CIART, K22E, YETS2, Q3U1M7, LMF1, FOXK2, PUF60, RREB1, ZEP2, UD3A1, ZCCHV, PRRC1, SFSWA, PRD10, ERMP1, Q3UXF4, TMED1, ZBT45, Q569X9, LIN54, TASO2, RESF1, ZN652, NUFP2, KDM6B, Q5PRE9, Q5RIM6, RBM27, UTP18, Q5SUT0, MED13, Q5SXC4, SFR19, UIMC1, A1CF, SIN3A, CSK21, CAPR1, MEF2A, RBBP7, KLF3, NCOA2, USF1, CTCF, GATA6, TS101, HCFC1, ZN148, HIRA, LASP1, RAI1, MAFK, PRG2, SPTB2, SSXT, TAF6, UD19, NUP62, UD11, MEF2D, TIF1A, USF2, CDK13, JHD2C, HECD1, Q6DI81, SCAF8, NOMO1, FND3B, Q6NXL1, ZMIZ1, NSD3, UGGG1, ALG8, AHDC1, PTN23, PIGS, NUP98, NFRKB, GNAS1, ONEC2, FNBP4, CNOT1, NU188, SPCS3, PICAL, HUWE1, CPEB4, PRR14, ATX2L, NACC1, MCAF1, KANL1, NU214, PR40B, UBN2, TNC18, UBP2L, ZN598, Q80ZX0, DDX42, LPP, TET3, E41L5, SP130, ZC3HE, SUN2, EST2E, NCEH1, ARI5B, EMSY, TM260, RFOX2, TM209, KMT2C, ASPH, SRRM2, NUP54, CPSF7, TOX4, IFIX, CREST, Z385B, PIGT, PGLT1, YTHD3, KAT6A, ASXL2, ZN609, POGZ, SREK1, ZHX2, ZHX3, P20D1, MBNL2, RBM14, PIAS2, CNOT2, ITCH, DIDO1, EPC1, SCYL2, G6PE, TCRG1, BCOR, CCAR1, Q8CHB3, ADNP2, BICRL, EP400, PHC3, P66A, FWCH1, PDLI5, NUP42, ZMIZ2, BTD, UD3A2, ESRP2, TAF10, ZBT20, Q8K154, GT251, ALG3, BRD3, I2BPL, PO121, SF3A1, EST2A, SF3B4, Q8R084, ZBT44, MTSS1, TMED4, ZC3HA, UBQL1, NUP58, BRD8, ATX7, STAB2, RBM12, RBPS2, MED25, MAVS, ALG12, HNRL1, CDIPT, SRSF4, P66B, TAF9, MCR, SFPQ, MBOA5, UBAP2, SMAP1, NCOA5, RBM47, CREL1, SC16B, BAZ2A, RBM5, RISC, ALS2, BCL7B, TMCO1, SYDC, CIC, MED15, WAC, MED1, GORS2, RBM10, ZN281, MLXPL, ANR17, ZN318, TRI33, PCYOX, NECP1, RBM33, SSRA, CREL2, PINX1, INT12, SP2, PHF14, SUN1, APMAP, FIP1, AP2B1, RPN2, LMAN2, AKAP8, MYPT1, RSRC1, EIF3F, Q9EQC8, ERAP1, SALL1, Q9ERL0, RBP2, RTN3, PALLD, TF2H2, ANM1, NUP50, HAKAI, HYOU1, ELOV1, ZN207, DOPP1, CCNT1, TBL1X, PO210, VKGC, QKI, UBQL2, HIPK2, COP1, PR40A, FOXO1, PIGN, MAN1, GANP, ENTP5, NFAT5, CARM1, FOXO3, FBLN5, IF2H, Q9Z1A1, DEAF1, HTAI2, HNRPF, ITPR2, S4R1W8, V9GX43
Species: Mus musculus
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Song J, Liu C, Wang X, Xu B, Liu X, Li Y, Xia J, Li Y, Zhang C, Li D, Sun H. O-GlcNAcylation Quantification of Certain Protein by the Proximity Ligation Assay and Clostridium perfringen OGA(D298N)(CpOGA(D298N)). ACS chemical biology 2021 16(6) 34105348
Abstract:
O-GlcNAcylation is an O-linked β-N-acetyl-glucosamine (O-GlcNAc)-monosaccharide modification of serine or threonine in proteins that plays a vital role in many critical cellular processes. Owing to its low molecular weight, uncharged property, and difficulty in distinguishing from β-N-acetyl-galactosamine (GalNAc), the lack of high specificity and avidity tools and sophisticated quantification methods have always been the bottleneck in analyzing O-GlcNAc functions. Here, we compared glycan array data of the mutant of Clostridium perfringen OGA (CpOGAD298N), O-GlcNAc antibody CTD110.6, and several lectins. We found that CpOGAD298N can effectively distinguish GlcNAc from GalNAc. Glycan array analysis and isothermal titration calorimetry (ITC) show that CpOGAD298N has a GlcNAc specific binding characteristic. CpOGAD298N could be used in far-western, flow cytometry analysis, and confocal imaging to demonstrate the existence of O-GlcNAc proteins. Using the CpOGAD298N affinity column, we identified 84 highly confident O-GlcNAc modified peptides from 82 proteins in the MCF-7 cell line and 33 highly confident peptides in 33 proteins from mouse liver tissue; most of them are novel O-GlcNAc proteins and could not bind with wheat germ agglutinin (WGA). Besides being used as a facile enrichment tool, a combination of CpOGAD298N with the proximity ligation assay (PLA) is successfully used to quantify O-GlcNAc modified histone H2B, which is as low as femtomoles in MCF-7 cell lysate. These results suggest that CpOGAD298N is a specific tool for detection (far-western, flow cytometry analysis, and confocal imaging) and enrichment of O-GlcNAcylated proteins and peptides, and the CpOGAD298N-PLA method is useful for quantifying certain O-GlcNAc protein.
O-GlcNAc proteins:
FSIP2, DYTN, P121C, ANM5, RGRF2, MSI1H, SNX2, IDHC, BAZ1A, AT10B, DDAH2, ADH1, ASSY, APOB, PPBT, SRC, K1C18, INVO, TRY1, A1AT1, O5AL1, PYC, ITPR1, GLU2B, ASSY, SON, DRD4, H2B1O, CP2DA, CXCR1, DHE3, MAP4, TRY3, BASI, LMNA, NU153, BRCA2, H2B1D, NAL11, CH60, ACTC, PI42B, HRH2, FKBP4, ANK3, ATM, UBP2L, ADRM1, TEN4, PAN3, FSIP2, TGO1, COA6, FRY, MYOME, SHE, HCFC1, ZN148, Q63800, SBP2, DYH17, A2MG, IQCE, AEDO, FBX38, QSOX2, NRAP, CNDG2, THIM, LONM, CLC10, MFS6L, DSEL, HMCS1, TACO1, CNTRB, NUP93, S2541, KCD17, MB213, CFA43, STAB1, SMRC2, DTX3L, GANC, GRK7, TRIM7, F227B, ADAD1, ADCYA, ERP44, FANCJ, TMM59, TBB2B, SPIT4, AP2B1, NUD12, I2BPL, CARD9, PABP3, ABHGB, WDCP, TDRD3, SUCHY, DCA13, KI21B, HEBP1, CTNL1, UBQL2, CAD22, TNIK, WDR3, RBM7
Species: Rattus sp, Homo sapiens, Mus musculus
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