O-GlcNAc regulates gene expression by controlling detained intron splicing
Open accessPublished version of a preprint
Abstract
Intron detention in precursor RNAs serves to regulate expression of a substantial fraction of genes in eukaryotic genomes. How detained intron (DI) splicing is controlled is poorly understood. Here, we show that a ubiquitous post-translational modification called O-GlcNAc, which is thought to integrate signaling pathways as nutrient conditions fluctuate, controls detained intron splicing. Using specific inhibitors of the enzyme that installs O-GlcNAc (O-GlcNAc transferase, or OGT) and the enzyme that removes O-GlcNAc (O-GlcNAcase, or OGA), we first show that O-GlcNAc regulates splicing of the highly conserved detained introns in OGT and OGA to control mRNA abundance in order to buffer O-GlcNAc changes. We show that OGT and OGA represent two distinct paradigms for how DI splicing can control gene expression. We also show that when DI splicing of the O-GlcNAc-cycling genes fails to restore O-GlcNAc homeostasis, there is a global change in detained intron levels. Strikingly, almost all detained introns are spliced more efficiently when O-GlcNAc levels are low, yet other alternative splicing pathways change minimally. Our results demonstrate that O-GlcNAc controls detained intron splicing to tune system-wide gene expression, providing a means to couple nutrient conditions to the cell's transcriptional regime.
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Cites
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566 · cited 1× · see citing works
“5 h) (64); both of these factors would dampen the impact of splicing changes on productive mRNA levels at short time points.”
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Self-citationMS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics
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- Authors
- Tan, Z.-W., Fei, G., Paulo, J. A., Bellaousov, S., Martin, S. E. S., Duveau, D. Y., Thomas, C. J., Gygi, S. P., Boutz, P. L., & Walker, S.
- Affiliations
- Harvard University (US)
- Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA
- University of Rochester Medicine (US)
- National Institutes of Health (US)
- Corresponding author
- Boutz, Paul L
- Walker, Suzanne
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2020-04-24
- Volume
- 48
- Issue
- 10
- Pages
- 5656-5669
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC7261177
- OpenAlex
- W3020244548
- Cited by
- 119
- References
- 3
- Citations by year
- 2026: 12 · 2025: 28 · 2024: 22 · 2023: 16 · 2022: 12 · 2021: 21 · 2020: 8
- FWCI
- 4.62
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nucleic Acids Research (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nd)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (GM094263, BB123456, GM034277)
- A*STAR
- University of Rochester Health Sciences Center
- National Center for Advancing Translational Sciences
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- O-GlcNAc, O-GlcNAc transferase, O-GlcNAcase, intron retention, alternative splicing, gene expression regulation, post-translational modification, nutrient signaling, mRNA levels
- MeSH terms
- RNA Splicing Factors, RNA-Seq, Acetylglucosamine, Cell Line, Glycoside Hydrolases, Humans, Introns, Phosphorylation, RNA Splicing, RNA, Messenger, N-Acetylglucosaminyltransferases, HEK293 Cells
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