REFERENCES


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Zhang X, Wang L, Lak B, Li J, Jokitalo E, Wang Y. GRASP55 Senses Glucose Deprivation through O-GlcNAcylation to Promote Autophagosome-Lysosome Fusion. Developmental cell 2018 45(2) 29689198
Abstract:
The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway. However, how the Golgi responds to glucose deprivation is so far unknown. Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions. Glucose deprivation reduces GRASP55 O-GlcNAcylation. De-O-GlcNAcylated GRASP55 forms puncta outside of the Golgi area, which co-localize with autophagosomes and late endosomes/lysosomes. GRASP55 depletion reduces autophagic flux and results in autophagosome accumulation, while expression of an O-GlcNAcylation-deficient mutant of GRASP55 accelerates autophagic flux. Biochemically, GRASP55 interacts with LC3-II on the autophagosomes and LAMP2 on late endosomes/lysosomes and functions as a bridge between LC3-II and LAMP2 for autophagosome and lysosome fusion; this function is negatively regulated by GRASP55 O-GlcNAcylation. Therefore, GRASP55 senses glucose levels through O-GlcNAcylation and acts as a tether to facilitate autophagosome maturation.
O-GlcNAc proteins:
GORS2, GORS2
Species: Homo sapiens, Rattus norvegicus
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Rexach JE, Rogers CJ, Yu SH, Tao J, Sun YE, Hsieh-Wilson LC. Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags. Nature chemical biology 2010 6(9) 20657584
Abstract:
Mechanistic studies of O-GlcNAc glycosylation have been limited by an inability to monitor the glycosylation stoichiometries of proteins obtained from cells. Here we describe a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags. This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels. In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry. Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods. We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
O-GlcNAc proteins:
SP1, SYN1, CREB1, NUP62, MECP2, SYN2, OGA, GORS2
Species: Homo sapiens, Rattus norvegicus
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Clark PM, Dweck JF, Mason DE, Hart CR, Buck SB, Peters EC, Agnew BJ, Hsieh-Wilson LC. Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins. Journal of the American Chemical Society 2008 130(35) 18683930
Abstract:
We report an advanced chemoenzymatic strategy for the direct fluorescence detection, proteomic analysis, and cellular imaging of O-GlcNAc-modified proteins. O-GlcNAc residues are selectively labeled with fluorescent or biotin tags using an engineered galactosyltransferase enzyme and [3 + 2] azide-alkyne cycloaddition chemistry. We demonstrate that this approach can be used for direct in-gel detection and mass spectrometric identification of O-GlcNAc proteins, identifying 146 novel glycoproteins from the mammalian brain. Furthermore, we show that the method can be exploited to quantify dynamic changes in cellular O-GlcNAc levels and to image O-GlcNAc-glycosylated proteins within cells. As such, this strategy enables studies of O-GlcNAc glycosylation that were previously inaccessible and provides a new tool for uncovering the physiological functions of O-GlcNAc.
O-GlcNAc proteins:
A0A0G2JYI7, A0A0G2K931, A0A0G2KAS9, ROA2, OTUB1, SEP11, B5DFG5, D3ZM69, HCFC1, D3ZQM0, D3ZUY8, D3ZVQ0, D4A0B4, D4A133, D4A1L2, D4A554, D4AA63, D4ABT8, D4ACB8, E9PT29, E9PTR4, S2512, RPGF2, F1M3L4, F1M3W5, F1M7Y3, F1M8R0, F1M949, F1M9V7, G3V7M0, G3V8Q8, HNRPC, SERA, AMPH, DCLK1, NCDN, CTND2, DNM1L, PICAL, CLIP2, ANK3, PACS1, HSP74, BSN, PTN23, AATM, CRYAA, ROA1, ENOA, HXK1, ENOG, ODP2, ALDOC, GLNA, SYN1, SORL, PLCB1, ATPB, DHE3, KCC2A, AT2A2, PDIA3, KPYM, FAS, AATC, MTAP2, MAP1B, ATPA, SPTN1, PGK1, HMCS1, AP2A2, CSK21, PO3F1, DYN1, MK03, AINX, THOP1, PGAM1, VPP1, ODPA, DCTN1, MARCS, MAP1A, 1433B, DYHC1, TERA, RP3A, PFKAM, PFKAP, ANXA6, TPIS, ODPB, NU153, GDIA, HUWE1, PYGB, GBB1, SNAA, NCKP1, OGT1, ACTB, HNRPK, 1433G, RS8, 1433E, RL7A, EF1A1, ACTA, VATB2, RS3, AP2B1, CH60, RACK1, PP2BA, KAPCB, 1433T, EF2K, VDAC2, GNAQ, TBB2A, FSCN1, ARPC2, CAND1, AP180, ADT1, ANXA2, ADT2, MYPT1, MIC60, TBB2B, CARM1, SRPRB, RD23B, TBB3, RBMX, OXR1, Q4V8F6, ZFR, WASF1, E41L5, RUFY3, DTBP1, SHLB2, Q5RJQ1, WDR1, IF4A2, CAPZB, ODO1, TBA4A, TCPB, SPTB2, 4EBP1, CAPS1, SYNJ1, DPYL1, DPYL4, DPYL3, CAMKV, KCC1A, MAP6, NDUS2, BACH, HS105, NDUS1, MAVS, PURB, QCR1, Q6AY07, Q6AYI1, PLAK, TBB4B, ROA3, Q6XLI7, PGAP1, FMR1, RB6I2, COR1A, IDH3A, PABP1, TALDO, DPYL5, WNK1, RIMS1, SEPT5, UBQL1, PCLO, MYH10, Q9JMB3, NSF, FKBP4, SHAN2, SRCN1, MYO5A, CRYM, GORS2, E41L1, GUAD, SEPT7, PACN1, Q9Z1X8, HOME1, GIT1, CTBP1, SC31A
Species: Mus musculus, Bos taurus, Rattus norvegicus
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Khidekel N, Ficarro SB, Peters EC, Hsieh-Wilson LC. Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain. Proceedings of the National Academy of Sciences of the United States of America 2004 101(36) 15340146
Abstract:
The covalent modification of intracellular proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) is emerging as a crucial regulatory posttranslational modification akin to phosphorylation. Numerous studies point to the significance of O-GlcNAc in cellular processes such as nutrient sensing, protein degradation, and gene expression. Despite its importance, the breadth and functional roles of O-GlcNAc are only beginning to be elucidated. Advances in our understanding will require the development of new strategies for the detection and study of O-GlcNAc-modified proteins in vivo. Herein we report the direct, high-throughput analysis of O-GlcNAc-glycosylated proteins from the mammalian brain. The proteins were identified by using a chemoenzymatic approach that exploits an engineered galactosyltransferase enzyme to selectively label O-GlcNAc proteins with a ketone-biotin tag. The tag permits enrichment of low-abundance O-GlcNAc species from complex mixtures and localization of the modification to short amino acid sequences. Using this approach, we discovered 25 O-GlcNAc-glycosylated proteins from the brain, including regulatory proteins associated with gene expression, neuronal signaling, and synaptic plasticity. The functional diversity represented by this set of proteins suggests an expanded role for O-GlcNAc in regulating neuronal function. Moreover, the chemoenzymatic strategy described here should prove valuable for identifying O-GlcNAc-modified proteins in various tissues and facilitate studies of the physiological significance of O-GlcNAc across the proteome.
O-GlcNAc proteins:
A3E0T0, HCFC1, D4A3Q3, D4A543, RPGF2, BSN, CRYAA, MTAP2, MAP1B, ATF2, TLE4, Q498M7, AGFG1, ZFR, NFRKB, WNK1, SPTN2, GORS2, E41L1, SYNPO
Species: Mus musculus, Bos taurus, Rattus norvegicus
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