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Akan I, Halim A, Vakhrushev SY, Clausen H, Hanover JA. Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes. Cells 2021 10(5) 33925313
Abstract:
The reversible posttranslational O-GlcNAc modification of serine or threonine residues of intracellular proteins is involved in many cellular events from signaling cascades to epigenetic and transcriptional regulation. O-GlcNAcylation is a conserved nutrient-dependent process involving two enzymes, with O-GlcNAc transferase (OGT) adding O-GlcNAc and with O-GlcNAcase (OGA) removing it in a manner that's protein- and context-dependent. O-GlcNAcylation is essential for epigenetic regulation of gene expression through its action on Polycomb and Trithorax and COMPASS complexes. However, the important role of O-GlcNAc in adult life and health span has been largely unexplored, mainly due the lack of available model systems. Cataloging the O-GlcNAc proteome has proven useful in understanding the biology of this modification in vivo. In this study, we leveraged a recently developed oga knockout fly mutant to identify the O-GlcNAcylated proteins in adult Drosophilamelanogaster. The adult O-GlcNAc proteome revealed many proteins related to cell and organismal growth, development, differentiation, and epigenetics. We identified many O-GlcNAcylated proteins that play a role in increased growth and decreased longevity, including HCF, SIN3A, LOLA, KISMET, ATX2, SHOT, and FOXO. Interestingly, oga mutant flies are larger and have a shorter life span compared to wild type flies, suggesting increased O-GlcNAc results in increased growth. Our results suggest that O-GlcNAc alters the function of many proteins related to transcription, epigenetic modification and signaling pathways that regulate growth rate and longevity. Therefore, our findings highlight the importance of O-GlcNAc in growth and life span in adult Drosophila.
O-GlcNAc proteins:
A0A0B4K6K9, A0A0B4K6N5, A0A0B4K6T1, A0A0B4K707, A0A0B4K7Q3, A0A0B4K7V4, A0A0B4K813, A0A0B4K880, A0A0B4KF23, A0A0B4KGY9, A0A0B4KHB2, A0A0B4KI71, A0A0B4LF93, A0A0B4LFP7, A0A0B4LFX4, A0A0B4LGJ1, A0A0B4LGL0, A0A0B4LH23, A0A0B4LH64, A0A0B4LHK4, A0A0B4LHS9, A0A0B4LIF3, A0A0B4LJ24, PO210, A1Z6M0, A1Z7F1, A1Z7Y7, A1Z8Z3, A1Z9J3, A1Z9L2, A8DQW8, SBNO, B7Z049, B7Z0L0, B7Z0Q5, E1JHV7, E2QCS7, G3JX32, M9MRJ4, M9MRN7, M9MS77, M9NCQ1, M9NE59, M9NEL3, M9NG31, M9NG33, M9NGK3, M9PCF6, M9PCJ8, M9PCM8, M9PCM8, M9PDU2, M9PE74, M9PEK8, M9PFU6, M9PI47, M9PI58, M9PI84, M9PJ79, O61380, O96607, RPB1, OPS1, L2GL, CO4A1, LAMB1, ITBX, LSP1G, ITA2, PDE4B, FSH, CYPR, DHGL, SUZ2, GLT, MNB, STIM, YL, LAMA, Q0E8B8, MESH, LSP2, SYN, Q5BIJ2, Q6GV06, SODE, Q7JWQ7, NUP62, NUP50, Q7K1C5, Q7K3Y9, Q7K3Z3, SCRIB, Q7KTJ7, LOLA4, PPN, Q86BM5, Q8IHB0, Q8IMB8, Q8IMH4, Q8INE9, Q8IPG9, TRR, LBR, Q8MMD3, Q8MRI4, Q8SWX4, Q8SX98, Q8SXR1, Q8T0N3, Q8T3W8, Q95R71, GILT1, Q95RC5, FOXO, CAPR1, Q9I7M5, Q9I7S9, LAR4, Q9I7T8, PATJ, CAPS, ERO1L, Q9V3U6, Q9V4B8, HCF, NUP54, Q9V9U1, CTNS, Q9VCR9, Q9VCS4, Q9VDI1, Q9VDT5, Q9VFC9, Q9VFR2, Q9VG78, Q9VH63, Q9VHC3, Q9VHC8, Q9VIF2, Q9VII5, Q9VJQ3, Q9VJX4, EDC4, Q9VKM8, Q9VKP2, Q9VKT1, Q9VLF4, Q9VM55, Q9VMD2, TIG, Q9VMV5, Q9VP57, Q9VPQ7, Q9VPU9, Q9VQ58, Q9VQM0, INE, Q9VR69, Q9VRT5, Q9VS02, Q9VSC3, JARD2, Q9VTC1, PLOD, Q9VTW7, NPLP2, Q9VUH6, Q9VUJ4, Q9VVP9, Q9VW34, Q9VWL4, MINY3, Q9VXA3, NU153, Q9VXH7, MADD, Q9VXY5, Q9VY04, Q9VYR1, Q9VZ58, Q9VZJ3, Q9VZQ7, Q9W1A9, Q9W1J0, NU214, Q9W2N6, Q9W329, Q9W3F3, Q9W3G1, Q9W3L4, Q9W3V9, Q9W451, Q9W4M7, FUTSC, Q9W5B4, Q9Y0Z1, Q9Y136, Q9Y141, Q9Y154, R9PY26, X2JAR4, X2JC54, X2JG40, X2JIM3
Species: Drosophila melanogaster
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Klement E, Lipinszki Z, Kupihár Z, Udvardy A, Medzihradszky KF. Enrichment of O-GlcNAc modified proteins by the periodate oxidation-hydrazide resin capture approach. Journal of proteome research 2010 9(5) 20146544
Abstract:
A chemical derivatization approach has been developed for the enrichment of O-GlcNAc modified proteins. The procedure is based on the isolation technique used for N-glycoproteins with appropriate modifications because of the differences in the two types of glycosylation: a prolonged periodate oxidation is followed by hydrazide resin capture, on-resin proteolytic digestion, and release of the modified peptides by hydroxylamine. This enrichment strategy offers a fringe benefit in mass spectrometry analysis. Upon collisional activation, the presence of the open carbohydrate ring leads to characteristic fragmentation facilitating both glycopeptide identification and site assignment. The enrichment protocol was applied to the Drosophila proteasome complex previously described as O-GlcNAc modified. The O-GlcNAc modification was located on proteasome interacting proteins, deubiquitinating enzyme Faf (CG1945) and a ubiquitin-like domain containing protein (CG7546). Three other proteins were also found GlcNAc modified, a HSP70 homologue (CG2918), scribbled (CG5462) and the 205 kDa microtubule-associated protein (CG1483). Interestingly, in the HSP70 homologue the GlcNAc modification is attached to an asparagine residue of a N-glycosylation motif.
O-GlcNAc proteins:
B7Z0D3, CRYAA, MA205, FAF, SCRIB
Species: Drosophila melanogaster, Bos taurus
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