HuR binds a cyclic nucleotide‐dependent, stabilizing domain in the 3′ untranslated region of Na+/glucose cotransporter (SGLT1) mRNA

FEBS Letters

Loflin, Paul¹  Lever, Julia E¹ 

[1] Department of Biochemistry and Molecular Biology, University of Texas-Houston Medical School, P.O. Box 20708, Houston, TX 77225, USA

关键词: mRNA stability;    Glucose transporter;    cAMP;    RNA binding protein;    Kidney epithelial cell;    SGLT;    Na+-coupled glucose transporter;    IBMX;    3-isobutyl-1-methylxanthine;    UTR;    untranslated region;    URE;    U-rich element;    nt;    nucleotide(s);   

DOI  :  10.1016/S0014-5793(01)03176-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown