HuR binds a cyclic nucleotide‐dependent, stabilizing domain in the 3′ untranslated region of Na+/glucose cotransporter (SGLT1) mRNA
Abstract
Differentiation‐dependent expression of the Na+/glucose cotransporter (SGLT1) is accompanied by a large, cAMP‐dependent increase in stability of its mRNA. Stabilization is mediated by protein binding to a critical uridine‐rich element (URE) in its 3′ untranslated region. In the present study, we demonstrate that HuR, an RNA binding protein of the embryonic lethal abnormal vision family, binds the SGLT1 URE. HuR binding was increased after elevation of intracellular cAMP levels and was dependent on protein phosphorylation. This interaction was prevented by a substitution mutation previously shown to block cAMP‐dependent reporter message stabilization. These results implicate HuR as a key mediator of cAMP‐dependent SGLT1 mRNA 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 [56]
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References 37 · Cited by 51
- Authors
- Loflin, P., & Lever, J. E.
- Corresponding author
- Lever, Julia E
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2001-11-27
- Volume
- 509
- Issue
- 2
- Pages
- 267-271
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2153193631
- Cited by
- 51
- References
- 37
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 3 · 2016: 1 · 2015: 4 · 2014: 2 · 2013: 2
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Connecticut
- Federation of European Biochemical Societies
- National Institutes of Health
- 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 › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- HuR, SGLT1, Na+/glucose cotransporter, mRNA stability, 3' untranslated region, cAMP signaling, protein phosphorylation, RNA-binding proteins
- MeSH terms
- ELAV-Like Protein 1, Cyclic AMP, Animals, Antigens, Surface, Cell Differentiation, Epithelial Cells, Humans, Kidney Tubules, Proximal, Membrane Glycoproteins, Monosaccharide Transport Proteins, Phosphorylation, Protein Binding, Recombinant Proteins, Swine, Up-Regulation, RNA-Binding Proteins, 3' Untranslated Regions, RNA Stability, Sodium-Glucose Transporter 1, ELAV Proteins
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