Cyclic nucleotide regulation of Na+/glucose cotransporter (SGLT1) mRNA stability
Open accessAbstract
Expression of the Na(+)-coupled glucose cotransporter SGLT1 is regulated post-transcriptionally at the level of mRNA stability. We have previously demonstrated that cAMP-dependent stabilization of the SGLT1 message was correlated with the protein phosphorylation-dependent binding of cytoplasmic proteins to a uridine-rich sequence (URE) in the 3'-untranslated region (UTR). In the present study, the regulatory role of the URE was demonstrated by inserting it into the 3'-UTR of a beta-globin reporter minigene under the control of the tetracycline-regulated promoter. The resultant chimeric globin/SGLT1 mRNA expressed after transfection into LLC-PK1 cells exhibited a decreased half-life compared with the beta-globin control, indicating that the URE serves a destabilizing function. Activation of protein kinase A stabilized the chimeric message but not the beta-globin control, indicating the presence of a regulatory stabilizing sequence within the URE. A 38-kDa nucleocytoplasmic protein was identified that recognized a 12-nucleotide binding site within the URE. A mutation in this binding site that prevented protein binding assayed in vitro by UV cross-linking also prevented protein kinase A-dependent stabilization of the chimeric message assayed in vivo. These findings identify the interaction between a 38-kDa nucleocytoplasmic protein and a regulatory uridine-rich sequence in the 3'-UTR as critical for cAMP-mediated SGLT1 message stabilization.
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An increase in SGLT-1 protein in the apical brush border of enterocytes occurs in a cAMP-dependent manner in response to basolateral signals, and secondary to increased SGLT-1 transcription and stabilization of the SGLT-1 transcript.
“An increase in SGLT-1 protein in the apical brush border of enterocytes occurs in a cyclic AMP (cAMP)-dependent manner in response to transduction of basolateral signals (54,55), and secondary to an increase in SGLT-1 transcription (56) and stabilization (increased half-life) of the 3 ′ -untranslated region of the SGLT-1 transcript (57,58).”
From Gut mechanisms linking intestinal sweet sensing to glycemic control (2018) · cites this paper as [57]
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- Authors
- Lee, W. Y., Loflin, P., Clancey, C. J., Peng, H., & Lever, J. E.
- Corresponding author
- Lever, Julia E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 275
- Issue
- 43
- Pages
- 33998-34008
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2081971539
- Cited by
- 26
- References
- 52
- Citations by year
- 2026: 1 · 2025: 1 · 2023: 1 · 2022: 1 · 2020: 1 · 2018: 2 · 2016: 1 · 2015: 1
- FWCI
- 1.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 27400)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- SGLT1, Na+/glucose cotransporter, mRNA stability, post-transcriptional regulation, cyclic AMP, protein kinase A, 3' untranslated region, mRNA destabilization, LLC-PK1 cells, protein phosphorylation
- MeSH terms
- Cyclic AMP, Animals, Binding Sites, Cell Line, Cell Nucleus, Cytoplasm, Membrane Glycoproteins, Monosaccharide Transport Proteins, RNA, RNA, Messenger, Swine, Tetradecanoylphorbol Acetate, 1-Methyl-3-isobutylxanthine, Protein Structure, Secondary, Cyclic AMP-Dependent Protein Kinases, 3' Untranslated Regions, Sodium-Glucose Transporter 1
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