Next Article in Journal
Identification of CTLA-4-Positive Cells in the Human Tonsil
Next Article in Special Issue
Glycosylation of Immune Receptors in Cancer
Previous Article in Journal
Efferocytosis Mediated Modulation of Injury after Neonatal Brain Hypoxia-Ischemia
Previous Article in Special Issue
Placental Glycoredox Dysregulation Associated with Disease Progression in an Animal Model of Superimposed Preeclampsia
Article

Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes

1
Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
2
Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and Odontology, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark
*
Author to whom correspondence should be addressed.
Academic Editor: Hamed Jafar-Nejad
Cells 2021, 10(5), 1026; https://doi.org/10.3390/cells10051026
Received: 31 January 2021 / Revised: 19 April 2021 / Accepted: 25 April 2021 / Published: 27 April 2021
(This article belongs to the Special Issue Glycosylation and Deglycosylation in Animal Development)
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. View Full-Text
Keywords: O-GlcNAc proteome; growth; short life span; HCF; KISMET; SIN3A; FOXO O-GlcNAc proteome; growth; short life span; HCF; KISMET; SIN3A; FOXO
Show Figures

Figure 1

MDPI and ACS Style

Akan, I.; Halim, A.; Vakhrushev, S.Y.; Clausen, H.; Hanover, J.A. Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes. Cells 2021, 10, 1026. https://doi.org/10.3390/cells10051026

AMA Style

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):1026. https://doi.org/10.3390/cells10051026

Chicago/Turabian Style

Akan, Ilhan; Halim, Adnan; Vakhrushev, Sergey Y.; Clausen, Henrik; Hanover, John A. 2021. "Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes" Cells 10, no. 5: 1026. https://doi.org/10.3390/cells10051026

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop