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Massman LJ, Pereckas M, Zwagerman NT, Olivier-Van Stichelen S. O-GlcNAcylation Is Essential for Rapid Pomc Expression and Cell Proliferation in Corticotropic Tumor Cells. Endocrinology 2021 162(12) 34418053
Abstract:
Pituitary adenomas have a staggering 16.7% lifetime prevalence and can be devastating in many patients because of profound endocrine and neurologic dysfunction. To date, no clear genomic or epigenomic markers correlate with their onset or severity. Herein, we investigate the impact of the O-GlcNAc posttranslational modification in their etiology. Found in more than 7000 human proteins to date, O-GlcNAcylation dynamically regulates proteins in critical signaling pathways, and its deregulation is involved in cancer progression and endocrine diseases such as diabetes. In this study, we demonstrated that O-GlcNAc enzymes were upregulated, particularly in aggressive adrenocorticotropin (ACTH)-secreting tumors, suggesting a role for O-GlcNAcylation in pituitary adenoma etiology. In addition to the demonstration that O-GlcNAcylation was essential for their proliferation, we showed that the endocrine function of pituitary adenoma is also dependent on O-GlcNAcylation. In corticotropic tumors, hypersecretion of the proopiomelanocortin (POMC)-derived hormone ACTH leads to Cushing disease, materialized by severe endocrine disruption and increased mortality. We demonstrated that Pomc messenger RNA is stabilized in an O-GlcNAc-dependent manner in response to corticotrophin-releasing hormone (CRH). By affecting Pomc mRNA splicing and stability, O-GlcNAcylation contributes to this new mechanism of fast hormonal response in corticotropes. Thus, this study stresses the essential role of O-GlcNAcylation in ACTH-secreting adenomas' pathophysiology, including cellular proliferation and hypersecretion.
O-GlcNAc proteins:
GPTC8, ITB4, PTPRF, VIR, HMCN2, SETX, RTF1, MYH7B, FSIP2, TITIN, ARGAL, CO6A5, MMRN2, STOX1, PLXB2, AGRG4, F25A2, LOXH1, HMCN1, TM233, PIEZ1, TOPZ1, CE350, M3K19, RYR2, ACACB, RN213, CF251, ARHG5, BICRA, FOXM1, DLDH, PEX5, WRN, CELR1, PROM1, STK10, MYPC3, DTNB, IKKB, ACTN3, ALDOC, RPB1, LMNB1, MAP1B, HVM57, PAI1, MCM3, MIS, RGRF1, MSRE, CTND1, RB22A, ZO1, QOR, ANXA5, MSH6, EVC, KCNN2, DEPD5, NOE3, TBB4B, ROCK1, GSH1, G3BP1, ATS1, TBB5, NF1, PGBM, IF2P, FA8, GDF3, KCMA1, ZCH18, TANC1, NSUN7, SHRM4, FAT4, IGFN1, HMHA1, FA98A, SCRN3, CH048, K22E, SHLD2, BIG3, SDK1, BAHC1, SLMAP, TBCD9, RIMB3, DYH12, ITAD, CKAP2, IGS10, A3LT2, ITA1, HERC2, XIRP2, TR150, IQEC2, LRC8B, FAT2, S39AC, VP13A, MTUS1, GSTCD, TENS3, ACACA, UTP20, KLRA4, PAPOA, STAR3, EWS, KTN1, GRID1, DDX5, CP131, SEM3B, TLL1, MINT, CCPG1, BTF3, TPP2, RBL1, COBA2, TASOR, PDS5A, CE290, NAL14, A2MG, ZZZ3, FREM2, CPSF6, RPRD2, HEAT6, P4R3A, FIL1L, SNX6, GAPD1, PTN23, TRI37, MON1A, MSL1, SARM1, CENPE, DAPLE, TIAM2, UBE2O, KDM3B, SYNE1, CMYA5, FHOD3, TBB2A, MYCB2, SGO2, MCAF1, STAR9, CAPS1, PHF8, CUL9, CLAP1, ST18, SGSM2, TAF1, M18BP, UBP2L, FLNB, OFD1, PTHB1, PDK1, TMCO3, NRDC, MARF1, TM87B, UNC80, TCAF1, KTU, UBP43, CAPS2, ZN609, DOCK2, RHG24, NAKD2, LENG8, UFL1, CD158, CLASR, SSPO, SLTM, NAV1, FBX4, RFWD3, MICA3, STAU2, NEIL3, CCD14, DDX18, UBP45, AL1L1, CCD80, TF2H3, FYCO1, HNRPU, DYH5, DHX36, AGRV1, FLNC, REST, NDUS1, CREL1, CELR3, DYST, BRWD1, GOGA2, PDIA6, TM1L1, RT4I1, CSTN3, PRP19, TARA, UBP16, NOG2, MYO7B, BCDO2, RTN4, RRBP1, ZN318, DHX30, MITOS, RBM33, NARF, KLH35, ACSL3, SYRC, C16L2, NBEA, TBB3, XPO4, RBCC1, LRP1B, CAC1F, PRG4, BIR1B, SRCN1, SHRM3, ING1, MACF1, ACL7A, SMK2B, H17B6, RPGR, RHG07, MAST1, ADA11, TIM, PFKAP, IRAG1, DEMA, P2R3D, SETBP, NEK4, PLD1
Species: Mus musculus
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Chuh KN, Zaro BW, Piller F, Piller V, Pratt MR. Changes in metabolic chemical reporter structure yield a selective probe of O-GlcNAc modification. Journal of the American Chemical Society 2014 136(35) 25153642
Abstract:
Metabolic chemical reporters (MCRs) of glycosylation are analogues of monosaccharides that contain bioorthogonal functionalities and enable the direct visualization and identification of glycoproteins from living cells. Each MCR was initially thought to report on specific types of glycosylation. We and others have demonstrated that several MCRs are metabolically transformed and enter multiple glycosylation pathways. Therefore, the development of selective MCRs remains a key unmet goal. We demonstrate here that 6-azido-6-deoxy-N-acetyl-glucosamine (6AzGlcNAc) is a specific MCR for O-GlcNAcylated proteins. Biochemical analysis and comparative proteomics with 6AzGlcNAc, N-azidoacetyl-glucosamine (GlcNAz), and N-azidoacetyl-galactosamine (GalNAz) revealed that 6AzGlcNAc exclusively labels intracellular proteins, while GlcNAz and GalNAz are incorporated into a combination of intracellular and extracellular/lumenal glycoproteins. Notably, 6AzGlcNAc cannot be biosynthetically transformed into the corresponding UDP sugar-donor by the canonical salvage-pathway that requires phosphorylation at the 6-hydroxyl. In vitro experiments showed that 6AzGlcNAc can bypass this roadblock through direct phosphorylation of its 1-hydroxyl by the enzyme phosphoacetylglucosamine mutase (AGM1). Taken together, 6AzGlcNAc enables the specific analysis of O-GlcNAcylated proteins, and these results suggest that specific MCRs for other types of glycosylation can be developed. Additionally, our data demonstrate that cells are equipped with a somewhat unappreciated metabolic flexibility with important implications for the biosynthesis of natural and unnatural carbohydrates.
O-GlcNAc proteins:
A1BN54, A2A4Z1, A2A6U3, A2AFJ1, A2AG83, A2AL12, A2AMW0, A2AMY5, LAS1L, B1AU75, OTUD4, B7FAU9, B7ZP47, D3YUC9, D3YVJ7, SAFB1, D3Z4W3, E9PVC5, E9PZM7, E9Q066, E9Q2X6, E9Q310, E9Q5L7, E9Q7M2, E9Q986, F6T2Z7, G3UZ44, G3UZI2, G3X8Q0, G3X8Y3, G3X928, G3X972, G3X9V0, G5E8E1, H3BKK2, J3JS94, CAN2, DPYL2, AIP, HDAC1, MP2K3, GSH0, DHX15, ZW10, AKAP2, SLK, NMT1, E41L2, SRPK1, PARG, SPD2A, LDHA, ANXA2, RIR1, ANXA1, LMNB1, LEG1, G3P, TPIS, COF1, FAS, CBX3, BCAT1, MCM3, MAP4, FKBP4, HMGB2, AIMP1, MP2K1, SYWC, RANG, UBP4, PTN11, RAB5C, DNLI1, CAP1, STAT3, EPS15, PURA, MSH2, ALD2, PURA2, NEDD4, GFPT1, PCY1A, ICAL, HDGF, UBP10, ACTN4, EF2, TB182, SF3B6, PCBP1, PSME3, PFD3, HNRPK, MTPN, DNJA1, SUMO1, IF5A1, UB2L3, 1433T, HDAC2, ELAV1, 4EBP2, PYRG1, TCPB, BOP1, DAB2, XDH, UBA1, LARP7, CNN2, PP4R2, PSA, Q3TFP0, GUAA, METK2, FA98A, Q3TT92, UAP1L, NOL9, FUBP2, Q3U4W8, YRDC, NOL8, COBL1, CSTOS, LRRF1, Q3V3Y9, DDX17, MDC1, TENS3, Q5UE59, SRC8, SAMH1, KHDR1, SPB6, CAPR1, PAPS1, ASNS, LAP2B, LAP2A, PPM1G, CDC37, FXR1, HS105, PCBP2, KPCI, DDX3X, TSN, DBNL, CYTB, ZYX, RALY, SQSTM, TPP2, PUR2, PEAK1, NOP58, TPM4, LTV1, ZC11A, Q6P5B5, SMHD1, GGA2, TXLNA, JUPI2, UBE2O, LARP1, 2AAA, MTCH2, DEK, MBB1A, ATX2L, OTUB1, MAP6, AFTIN, FLNB, PI42B, ZN598, SAFB2, GRWD1, CPPED, LPP, PEF1, IF4B, Q8BGJ5, SYAC, RUFY1, PRUN1, CTF18, AHSA1, RCC2, IPO5, CKAP4, PPR18, HEAT3, SRRM2, HAT1, MAP1S, TLK1, CND2, THOP1, SEP11, TBL3, SEP10, UBA6, SYEP, GNL3, PDLI5, HMCS1, PKHO2, NEK9, ANLN, MATR3, CBR3, MEPCE, ERF3A, SPART, TDIF2, MCMBP, UBP15, MAVS, Q8VCQ8, PSMD2, FLNC, CPIN1, ACLY, MK67I, RINI, PUS7, CSDE1, DUS3L, KCC1A, TTC1, TADBP, RIN1, NONO, RRAGC, SERB, UBQL4, OGFR, NPM3, GLOD4, MTAP, CYB5B, PSMD9, CHSP1, OCAD1, RANB3, MFR1L, TBC15, CYBP, ZCHC8, GARS, CD37L, UB2V1, HNRPM, Q9D4G5, NOP56, IPYR, CNN3, KAP0, PLIN3, AKAP8, XRN2, MYPT1, PUR6, WDR4, SENP3, LIMA1, ANM1, NUP50, DDX20, IQGA1, MBNL1, ELOV1, DCLK1, BAG3, PPCE, CAF1A, LIMD1, DREB, TOM40, DEST, FOXO1, NFKB2, PDC6I, COR1C, TAGL2, CARM1, MTNB, GBP2, P5CS, EIF3G, SAE2, USO1, HNRPF, KEAP1
Species: Mus musculus
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