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Jaiswal R, Liu Y, Petriello M, Zhang X, Yi Z, Fehl C. A reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice. Glycobiology 2025 35(3) 39927985
Abstract:
A key nutrient sensing process in all animal tissues is the dynamic attachment of O-linked N-acetylglucosamine (O-GlcNAc). Determining the targets and roles of O-GlcNAc glycoproteins has the potential to reveal insights into healthy and diseased metabolic states. In cell studies, thousands of proteins are known to be O-GlcNAcylated, but reference datasets for most tissue types in animals are lacking. Here, we apply a chemoenzymatic labeling study to compile a high coverage dataset of quadriceps skeletal muscle O-GlcNAc glycoproteins from mice. Our dataset contains over 550 proteins, and > 80% of the dataset matched known O-GlcNAc proteins. This dataset was further annotated via bioinformatics, revealing the distribution, protein interactions, and gene ontology (GO) functions of these skeletal muscle proteins. We compared these quadriceps glycoproteins with a high-coverage O-GlcNAc enrichment profile from mouse hearts and describe the key overlap and differences between these tissue types. Quadriceps muscles can be used for biopsies, so we envision this dataset to have potential biomedical relevance in detecting aberrant glycoproteins in metabolic diseases and physiological studies. This new knowledge adds to the growing collection of tissues with high-coverage O-GlcNAc profiles, which we anticipate will further the systems biology of O-GlcNAc mechanisms, functions, and roles in disease.
O-GlcNAc proteins:
A0A087WS16, A0A0N4SUN5, A0A286YCS6, A0A5F8MPM4, A0A5F8MPQ4, A0A668KL51, A0A7N9VR94, A2A6J0, A2A6Q8, OBSCN, A2AEX6, A2AI87, A2AKD7, TITIN, KLH41, ARMT1, OSBL8, SHAN1, D3Z0V7, D3Z2B4, CD054, E0CZE0, E9PYG6, E9PYI8, E9PZD8, RYR1, E9Q1W3, NU153, E9Q3P4, RN213, E9Q616, TRDN, E9QL12, E9QN70, E9QND8, F6QYF8, F6VY18, F6YT88, F8VPN4, F8WGD9, MYH2, G3UYC5, RGS22, G3X972, AT2B1, G5E895, G5E8L1, G5E8R7, H7BWZ9, J3QN31, M0QW57, HXK2, CA2D1, PRDX6, DLDH, HCD2, MK12, SYPL1, CASQ1, PHB2, CAN1, CALU, CAVN1, IMPA1, NIPS2, AT2A2, PDLI3, PGAM2, PDLI1, RTN2, NTR1, WDR1, PLIN4, ZFR, SEM3F, ACTN3, SYPL2, CAH2, CO3, LAMC1, NU5M, ATP8, FABP4, MYG, ALDOA, KAPCA, AATC, AATM, TBA3, LDHA, MAOX, KCRM, ANXA2, A1AT1, SPA3K, HS90A, PHKG1, SODC, MDHM, ITB1, PDIA1, PGK1, MYL3, SODM, UBB, CALM3, ANXA1, EF1A1, CATB, TAU, GSTM1, H2B1F, H10, FINC, FABPH, DMD, COX5A, TNNI2, MYH3, MYH8, CAH1, GPDA, RL7, MDHC, HSPB1, ANXA6, GLNA, B4GT1, H12, CAH3, LEG1, LDHB, HS71L, G3P, ENOA, PPIA, TPIS, CATD, COF1, FAS, GSTP1, SERPH, COX5B, COX41, BIP, VIME, TNNC2, PLMN, ENOB, VTDB, CLK1, EST1C, RS2, TLN1, RADI, DHE3, FKB1A, MAP4, PLAP, PDIA3, ADHX, KCC2B, PGS2, MUG1, PABP1, DESM, AIMP1, PRVA, UBP4, ODPA, FAAA, PRDX1, RL12, HSPA9, CAP1, ACSL1, ECI1, STA5B, H14, H11, H15, H13, ALDR, COF2, ACADM, MYO1B, ALDH2, CAZA2, PFKAM, CACP, RL5, CBR1, ADT1, SAHH, CSRP3, ACADV, FMOD, ACADL, CAV3, ADT2, EAA3, AAAT, KPYM, CPT2, ODB2, MOT1, IDHP, STMN1, RD23B, PUR8, ADK, ACYP2, CX6B1, UBP5, ATPB, UCP3, EF2, TPM1, IRPL1, ACTB, CDC42, RAB5B, RAB10, UB2D1, 1433G, RS7, PP1B, 1433E, RS11, EF1A2, H4, RAB1A, RAN, RL23, CYC, RS3, YBOX1, RAC1, LIS1, HSP7C, CH60, 1433Z, HMGB1, IF5A1, ACTS, TBA4A, TBB4B, MP2K6, PEBP1, STIM1, HINT1, MYBPH, NACAM, TCPH, TCPB, TCPD, TCPE, TCPZ, SGCB, WNK1, ARF5, ISC2A, CSRP1, RS3A, SPSY, MYL11, FUMH, LYPA1, ARVC, PRDX5, XDH, NDKB, TERA, UBA1, CAC1S, ATPA, CO6A1, PGBM, PYC, ACADS, KCMA1, PADI2, CD36, Q14BI5, FAT4, CNNM3, Q3TCF3, PDLI7, PRC2C, SCRN3, DDB1, K0930, Q3UER8, LIMC1, PRRC1, EID3, AMPD1, Q561M1, MYPN, Q5F247, MLIP, Q5MJ56, CLU, MYH4, MYH1, UBR3, MYPC2, ODO1, LAMA2, COCA1, STIP1, REEP5, VDAC2, VDAC3, VDAC1, COQ8A, PRDX2, HCFC1, LAMB2, HSP74, HCDH, FBN1, GDIB, PZP, NNTM, DDX3X, MYOM1, SPEG, NDUA4, NUP62, AT2A3, GPDM, VINC, PUR2, CLH1, MYOF, HECD1, F120A, HELZ, Q6NVF7, IF4G1, Q6P1B9, Q6P6L5, KCRS, LPPRC, KMT2D, AT1A2, Q6S9I0, CAND1, CAND2, CMYA5, VWA2, TLN2, 2AAA, MIC27, Q7TPG0, MBB1A, SRCA, ATX2L, Q7TQS8, KPBB, Q80T54, NU214, PANK4, Q810Q0, EFTU, H2A3, LPP, PSD11, S2512, ECHM, EIF2A, ODPX, MAON, ODP2, ECHA, Q8BPI2, Q8BUY2, DHPR, SYP2L, THIM, STAC3, ASGL1, TLK1, PRR33, STBD1, MIC60, SYNPO, CPLN1, SYEP, UN45B, PGP, DRS7C, EI2BE, PDLI5, AGO3, EFGM, FIBB, COQ9, SDHA, VRK3, NNRE, HIBCH, THIL, AIMP2, BLMH, CMBL, UBQL1, TSN8, SLF1, CACB1, AT2A1, CLYBL, PRAF3, LSM1, MAVS, MYLK2, EST1D, MYH9, PSMD2, HNRL1, LMCD1, HNRPU, S25A3, FLNC, NDUS1, RINI, ATPG, DDX1, UBAP2, NDUS2, CISD1, SH319, HEMO, SYNP2, NDUV1, MYH7, PCCA, UGPA, ETFD, MACD1, C1TC, CLIP1, MPI, CPT1B, TALDO, THTM, GORS2, ECHB, ACON, NAMPT, 3HIDH, DHRS4, NDUAA, ETFA, PARK7, ASPN, MCCA, PPR3A, GDIR1, LGUL, NDUC2, DECR, NDUA2, SDHB, TMED6, GLRX3, AT5F1, ACO13, RL14, NDUB7, M2OM, UCRI, CHSP1, SFT2C, PUR9, SGT1, CENPV, SERB1, SPCS2, QCR1, NSF1C, CISY, ODPB, PGM1, SCOT1, GAL3A, RAB1B, ODO2, NDUV2, FUND2, IDH3A, RL4, EF1G, CA074, ATPO, PXL2B, QCR2, ACDSB, MYPT1, Q9DBT6, DCAF6, OCTC, NDUA9, NDUA8, PUR6, NDUBA, NDUS3, ETFB, ATP5H, MIC26, MMSA, RB27A, JPH2, JPH1, IVD, DYHC1, NIT2, ACTN2, MYOTI, PROF2, MYOZ1, PRELP, YBOX3, MBNL1, LDB3, HIG1A, TRXR1, B4GT5, PPCE, PLEC, S2513, NDRG2, DNJA2, UBQL2, FHL3, GLYG, ESTD, KAD1, PDC6I, PYGM, SUCA, ECI2, SH3BG, ARC1B, ABEC2, VAPA, AIFM1, GYS1, STRAP, LETM1, SUCB1, S4R1W1
Species: Mus musculus
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Lanzillotta C, Prestia F, Greco V, Iavarone F, Cordella F, Sette C, Forte E, Tramutola A, Lanzillotta S, Cassano T, Di Angelantonio S, Urbani A, Barone E, Perluigi M, Di Domenico F. Enhancing protein O-GlcNAcylation in down syndrome mice mitigates memory dysfunctions through the rescue of mitochondrial bioenergetics, stress responses and pathological markers. Redox biology 2025 85 40684658
Abstract:
Disturbances of the single sugar modification of proteins, O-GlcNAc, have been identified as a potential connection between disrupted brain metabolism and intellectual decay. In Alzheimer disease (AD), the reduced uptake of glucose in the brain results in aberrant O-GlcNAc cycling contributing to redox imbalance and neurodegeneration. Notably, alterations of O-GlcNAc homeostasis, associated with impaired O-GlcNAc transferase (OGT)/O-GlcNAcase (OGA) regulation, foster neuropathological mechanisms characterized by the presence of AD hallmarks in Down syndrome (DS) models. In the present study we examined the ability of Thiamet G (TMG), a well-known OGA inhibitor, in improving bio-energetic processes, inducing stress responses, reducing AD-related signatures and ameliorating cognition in a murine model of DS. Our data demonstrate that short-term intranasal administration of TMG restored OGA activity and normalized the global O-GlcNAc profile in mouse cortices. By a proteomic approach we identified protein components whose increased O-GlcNAc levels rescue, resulted to brain molecular and cognitive improvements. Remarkably, these included elements involved in energy production, neuronal architecture, antioxidant and stress response mechanisms. The ability of TMG in rescuing O-GlcNAc cycle and metabolic changes, associated with improved mitochondrial activity in cortical tissue, was further accompanied by changes in the O-GlcNAc/phospho ratio of APP and Tau. Functional improvements translated in enhanced recognition memory in Ts2Cje mice. Our study highlights the pivotal role of altered protein O-GlcNAcylation in DS neuropathology and establishes the molecular basis to envision the O-GlcNAc process as a promising therapeutic target to mitigate genetic- and metabolism-driven brain alterations linked to redox imbalance, mitochondrial failure and the development of AD features.
O-GlcNAc proteins:
APBA1, GDS1, DPYL2, STXB1, DLDH, DPYL4, REPS1, CTBP1, COR1A, GFAP, ALDOC, ALDOA, AATC, AATM, ENPL, NFL, NFM, PDIA1, TAU, KCC2A, NCAM1, ENOA, ENOG, HXK1, NFH, BIP, MAP4, KCRU, CTND1, DYN1, CAP1, TCPQ, NSF, PRS7, ALDH2, LMNA, SAHH, GDIA, KPYM, UBP5, ATPB, EF2, HNRPK, ABI2, LIS1, CH60, TBA4A, TBB4B, DLG3, TIAR, NHRF1, DPYL1, RGS14, TBB5, HNRL2, PLAK, ATPA, ANXA7, PPR21, FUBP2, CMPK2, GRIN1, C1TM, SRC8, TS101, PGCB, TCPW, DSG1A, FSCN1, PACN1, DLG4, SYN2, UBXN7, AT1A3, AT1A2, NEB2, 2AAA, TBB2A, PHF24, EFTU, PSD11, SAM50, MAON, CPNE3, SSDH, SEP11, MIC60, OGT1, PYGB, DNM1L, THIL, HNRPL, SHLB2, SNP47, FIBG, AT1A1, IRGQ, CSDE1, SYYC, PCY2, GMPPA, ARP3, RANB3, QCR1, SCOT1, TBB4A, EF1G, DPYL5, TBB3, LGI1, HABP4, AL9A1, GUAD, PDC6I, PYGM, E41L3, PACN2, P5CS, RASL1, PDPK1
Species: Mus musculus
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Ji S, Kang JG, Park SY, Lee J, Oh YJ, Cho JW. O-GlcNAcylation of tubulin inhibits its polymerization. Amino acids 2011 40(3) 20665223
Abstract:
The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction. Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line. We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin. Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively. We found that an increase in α-tubulin O-GlcNAcylation reduced heterodimerization and that O-GlcNAcylated tubulin did not polymerize into microtubules. Consequently, when O-GlcNAcase inhibitors were co-incubated with tRA, the extent of neurite outgrowth was decreased by 20% compared to control. Thus, our data indicate that the O-GlcNAcylation of tubulin negatively regulates microtubule formation.
O-GlcNAc proteins:
TBA1B, CTND1, YBOX1, TBA4A, TBA1A, TBB4B, TBA1C, FOXC1, NUP62, DDHD2, PSD11, NUP54, TBB6, TBB2B, TBB3, UBQL2
Species: Mus musculus
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