| RNA-binding protein HuR regulates RGS4 mRNA stability in rabbit colonic smooth muscle cells. | |
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MedLine Citation:
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PMID: 20881234 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Regulator of G protein signaling 4 (RGS4) regulates the strength and duration of G protein signaling and plays an important role in smooth muscle contraction, cardiac development, and psychiatric disorders. Little is known about the posttranscriptional regulation of RGS4 expression. We cloned the full-length cDNA of rabbit RGS4, which contains a long 3'-untranslated region (UTR) with several AU-rich elements (AREs). We determined whether RGS4 mRNA stability is mediated by the RNA-binding protein human antigen R (HuR) and contributes to IL-1β-induced upregulation of RGS4 expression. We show that IL-1β treatment in colonic smooth muscle cells doubled the half-life of RGS4 mRNA. Addition of RGS4 3'-UTR to the downstream of Renilla luciferase reporter induced dramatic reduction in the enzyme activity and mRNA expression of luciferase, which was attenuated by the site-directed mutation of the two 3'-most ARE sites. IL-1β increased luciferase mRNA stability in a UTR-dependent manner. Knockdown of HuR significantly aggravated UTR-mediated instability of luciferase and inhibited IL-1β-induced upregulation of RGS4 mRNA. In addition, IL-1β increased cytosolic translocation and RGS4 mRNA binding of HuR. These findings suggest that 3'-most ARE sites within RGS4 3'-UTR are essential for the instability of RGS4 mRNA and IL-1β promotes the stability of RGS4 mRNA through HuR. |
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Authors:
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Fang Li; Danielle Y Hu; Shu Liu; Sunila Mahavadi; William Yen; Karnam S Murthy; Kamel Khalili; Wenhui Hu |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2010-09-29 |
Journal Detail:
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Title: American journal of physiology. Cell physiology Volume: 299 ISSN: 1522-1563 ISO Abbreviation: Am. J. Physiol., Cell Physiol. Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-12-01 Completed Date: 2011-01-04 Revised Date: 2011-12-21 |
Medline Journal Info:
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Nlm Unique ID: 100901225 Medline TA: Am J Physiol Cell Physiol Country: United States |
Other Details:
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Languages: eng Pagination: C1418-29 Citation Subset: IM |
Affiliation:
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Department of Neuroscience, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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3' Untranslated Regions Animals Antigens, Surface / genetics, metabolism* Base Sequence Colon / metabolism* Humans Interleukin-1beta / metabolism*, pharmacology Molecular Sequence Data Myocytes, Smooth Muscle / metabolism* RGS Proteins / genetics, metabolism* RNA Stability* RNA-Binding Proteins / genetics, metabolism* Rabbits Up-Regulation |
| Grant Support | |
ID/Acronym/Agency:
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DK-015564/DK/NIDDK NIH HHS; DK-075964/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/3' Untranslated Regions; 0/Antigens, Surface; 0/ELAVL1 protein, human; 0/Interleukin-1beta; 0/RGS Proteins; 0/RNA-Binding Proteins; 175335-35-0/RGS4 protein |
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