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Chen CH, Lin KD, Ke LY, Liang CJ, Kuo WC, Lee MY, Lee YL, Hsiao PJ, Hsu CC, Shin SJ. O-GlcNAcylation disrupts STRA6-retinol signals in kidneys of diabetes. Biochimica et biophysica acta. General subjects 2019 1863(6) 30905621
Abstract:
O-GlcNAcylation is an important mechanism of diabetic complication. Retinoid homeostasis regulates cell-physiological functions through STRA6-retinol signaling. Therefore, we investigated whether O-GlcNAcylation disrupted STRA6-retinol signals in diabetes.
O-GlcNAc proteins:
AL1A1, STRA6
Species: Homo sapiens
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Berthier A, Vinod M, Porez G, Steenackers A, Alexandre J, Yamakawa N, Gheeraert C, Ploton M, Maréchal X, Dubois-Chevalier J, Hovasse A, Schaeffer-Reiss C, Cianférani S, Rolando C, Bray F, Duez H, Eeckhoute J, Lefebvre T, Staels B, Lefebvre P. Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex. Proceedings of the National Academy of Sciences of the United States of America 2018 115(47) 30397120
Abstract:
The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions. An interactomic approach identified O-GlcNAc transferase (OGT) as a REV-ERBα-interacting protein. By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity. We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus. AKT phosphorylation was inversely correlated to REV-ERBα expression. REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites. As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin. Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
O-GlcNAc proteins:
A4D111, POTEF, A5GZ75, AXA2L, P121C, A9Z0R7, EIFCL, C3UMV2, F1JVV5, I6TRR8, MYO1C, IF2B3, DDX3X, TCRG1, OPLA, XPO1, SC16A, SET1A, OGT1, EIF3D, DDX3Y, DHX15, PRP4, SERA, PSMD3, HNRPR, ACTN4, MYO1B, AKAP8, HNRPQ, UGDH, USO1, WDR1, ANR17, GGCT, LX12B, FLNB, PR40A, SF3B1, SPB7, NU155, KRT38, SC24D, GLSK, SC31A, ELP1, SMC2, AGM1, UTS2, BAG4, SC24A, SC24B, AP2A1, LDHA, AL1A1, PGK1, A2MG, CO3, CYTA, KV117, IGHG1, IGHA1, APOE, APOC2, FIBG, TFR1, TRFE, CATA, ALDOA, TBB4A, G3P, HSPB1, RPN1, RPN2, AT1A1, ARGI1, ALDH2, S10A8, ADT2, GELS, ATPB, APOA4, ENOA, PYGL, G6PI, PDIA1, CATD, ANXA2, CAN1, TBB5, HS90A, SP1, CO1A2, HS90B, PO2F2, GSTP1, VILI, ANXA4, PARP1, LKHA4, ATX1L, POTEI, UBB, UBC, SAA2, HS71A, HS71B, IGG1, TBA3C, TBA3D, THIO, CH60, BIP, HSP7C, PYGB, PYGM, G6PD, PYC, C1TC, NFH, IMDH2, XRCC6, XRCC5, AT1A3, EF2, PDIA4, P4HA1, ENOB, GFAP, ENPL, IDE, PO2F1, HNRPL, PLAK, DESP, AT2A2, HSP76, DDX5, LEG3, TCPA, RL7, VINC, E2AK2, ITIH2, ANXA7, HNF1A, FILA, CD11B, FLNA, VDAC1, TGM2, PUR2, UBA1, NDKB, TGM1, EST1, SFPQ, SAHH, MCM3, ATPA, PTBP1, SYVC, ABCD3, GRN, TKT, SPB3, AL4A1, PDIA3, KPYR, RPB2, AKT1, PUR9, HNRH1, CASPE, 1433S, S10AB, PRDX2, MCM4, MCM7, HS71L, CTNB1, IRS1, GDE, MYH9, FUS, SPB5, NUP62, TALDO, HSPA9, CAPG, TCPZ, STAT3, MDHC, MDHM, ECHA, GARS, SYIC, HUTH, LPPRC, MATR3, MSH2, VDAC2, SYQ, LEG7, COPD, SPB4, TCPE, AL9A1, LMAN1, FMO5, TCPG, SYAC, RBM25, KLK7, DYN2, TCPQ, TCPD, RAB7A, KS6A3, HNRPM, HXK2, CAZA1, NUP98, ACLY, COPB, COPA, SC24C, SYRC, SYYC, UBP14, HSP72, P5CS, XPO2, TERA, MTP, AF17, PSA, HNRH2, EIF3B, SYMC, NU107, EPIPL, TPIS, ACTB, IF4A1, HNRPK, 1433G, PRS4, ACTA, H4, RS27A, RL40, 1433Z, RACK1, ACTG, ACTH, ACTC, ACTS, TBA1B, TBA4A, TBB4B, PRKDC, DCD, VIGLN, CLH1, HNRPU, FABP5, MSHR, EWS, SEMG2, DSG1, SP3, PLOD1, EF1A2, GFPT1, PRDX1, KHDR1, TGM3, DHX9, LG3BP, DSC1, ILF3, TRAP1, PAK2, PSMD2, PABP4, PICAL, PKP1, BLMH, SNTB1, TBB2A, VEZF1, TRI29, UBP2L, LY6D, SRC8, PDIA5, HS902, EPN4, SMC1A, GANAB, MVP, PLEC, NONO, SC23A, SC23B, CDSN, JHD2C, CYTM, DPYL2, PCKGM, TKFC, Q53G76, Q58FF2, Q59EA0, ZN326, FILA2, UBAP2, KPLCE, RBM26, EF1A3, ARID2, TBA3E, POTEE, SBSN, FBX50, Q70T18, Q71E78, TBA1A, SND1, NUP54, MYH14, PEG10, PRP39, TAXB1, CAND1, CARM1, PRSR1, SPA12, ANKH1, ASXL1, NUP93, RDHE2, Q8N6B4, PDPR, TNR6A, COP1, PDC6I, POF1B, ATX2L, DDX1, BAP1, TFG, RBP56, EVPL, DDX17, RENT1, FUBP2, UBP7, NCLN, H2B1A, WNK4, ZC3HA, SCYL1, SPB12, GSDMA, VPS35, PHF12, CIC, STRBP, VAT1, NUP88, ATX2, CPNE1, TCPH, TBA1C, DIDO1, HNRL1, TBB2B, NUP58, ACTBM, TB182, SP130, WNK1, AGO3, MCCB, MOV10, TNR6C, S10AE, DD19A, ATD3A, TBA8, UGGG1, IF2B1, CALL5, RRBP1, NXF1, S2513, PO2F3, AGO2, AGO1, Q9UL79, ACSL5, DD19B, TNR6B, CD11A, EIF3L, SYFA, KLK5, RTCB, WNK2, PKP3, HYOU1, SNX9, COPG1, IF2B2, S23IP
Species: Homo sapiens
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Li S, Zhu H, Wang J, Wang X, Li X, Ma C, Wen L, Yu B, Wang Y, Li J, Wang PG. Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics. Electrophoresis 2016 37(11) 26853435
Abstract:
O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms. It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases. Despite its importance, identifying O-GlcNAcylated proteins is a major challenge in proteomics. Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells. In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne. After conjugation with click chemistry in vitro and enrichment via streptavidin resin, proteins with O-GlcNAc modification were separated by SDS-PAGE and identified with mass spectrometry. Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping. Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html). These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC. The proteomics credibility was also confirmed by the molecular function and cell component gene ontology (GO). Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
O-GlcNAc proteins:
AXA2L, EIFCL, MYO1C, P2Y10, IPO5, PLOD2, DDX3X, ZN197, XPO1, PPM1G, HNRPR, ACTN4, SNG2, OGA, UGDH, BRD4, FLNB, U520, IDHC, TOM70, K2C75, LDHA, AL1A1, DHE3, PGK1, PIGR, IGHA1, K1C14, K2C6A, LMNA, ALBU, TRFL, K2C6B, K2C1, AT1A1, ALDH2, S10A8, ITB1, K1C18, K2C8, ENOA, G6PI, HYEP, PDIA1, TBB5, SYEP, HS90A, 4F2, HS90B, VIME, K2C7, K1C16, RSSA, DLDH, PARP1, LIGO3, UBB, HS71A, CH60, BIP, HSP7C, PYGB, G6PD, C1TC, K2C3, ACTN1, PEPD, XRCC5, RINI, EF2, K1C10, K1C13, K2C5, PDIA4, P4HA1, GLU2B, KPYM, ENPL, HNRPL, PLAK, DESP, NCPR, AT2A2, NAGAB, HSP76, CAN2, NUCL, IF2B, ANXA7, FLNA, TGM2, PUR6, UBA1, SAHH, RPB1, ATPA, MOES, EF1G, CALR, MAP4, CALX, ITPI2, TKT, PDIA3, 2AAA, AL3A1, CPSM, QCR1, HNRH1, STIP1, HSP74, K1C9, MYH9, MYH10, K22E, PRS7, SRBP1, HSPA9, IF4A3, IF2G, LPPRC, MATR3, AL3B1, NAMPT, UBP5, KI67, MAP1B, UTRN, IQGA1, TCPE, K2C6C, AL9A1, NASP, FAS, TCPG, EFTU, SYAC, F10A1, TCPQ, TCPD, 6PGD, HNRPM, ACLY, SYRC, UBP14, S12A2, TERA, ECHB, NP1L1, EIF3B, SYMC, EIF3E, ACTB, UB2D3, ARP3, HNRPK, PRS4, ACTC, EF1A1, TBA1B, TBB4B, KRT85, PRKDC, DCD, S25A3, CLH1, HNRPU, SPTB2, PFKAP, FKBP4, AKA12, IF4G1, K1C17, CKAP4, DHX9, RBBP4, TP53B, TRAP1, PSMD2, SQSTM, TBB3, SPTN1, HNRPD, EIF3A, GANAB, GOGB1, IMB1, NUMA1, PDIA6, PLEC, PCM1, K1H1, KCC4, DREB, TRXR1, HKDC1, LRRF1, FILA2, BIG3, CROCC, BROX, K2C79, K2C80, PRP8, CCD81, SPT6H, SND1, MYH14, CC190, HORN, UNC80, GHDC, CDRT4, TXND5, NDRG1, GCN1, TNPO1, SIPA1, ERO1A, ODAD4, VPS35, ERP44, EHD4, SLK, RTN4, DDX21, SYFB, MYOF, RRBP1, SRP68, ACINU, SRRM2, PA2G4, MA2B2, RTCB, TLN1
Species: Homo sapiens
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Wang Z, Park K, Comer F, Hsieh-Wilson LC, Saudek CD, Hart GW. Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes. Diabetes 2009 58(2) 18984734
Abstract:
O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity. Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
O-GlcNAc proteins:
PHAR2, ATRN, AL1A1, CAH1, CAH2, HBD, SPTA1, B3AT, CATA, G3P, HS90A, GTR1, EPB41, PYGM, SPTB1, HEM2, ACPH, ANK1, EPB42, PSA5, AQP1, PRDX2, SYUA, HBB, HBA, GSTO1, PRDX1, NOM1, KCD18, VP13B, S29A1, S22AD
Species: Homo sapiens
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