ArticleThe Biochemical journal2001
Spot 14 protein interacts and co-operates with chicken ovalbumin upstream promoter-transcription factor 1 in the transcription of the L-type pyruvate kinase gene through a specificity protein 1 (Sp1) binding site.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 28 citations in OpenAlex.
- Effects of Branched-Chain Fatty Acids Derived from Yak Ghee on Lipid Metabolism and the Gut Microbiota in Normal-Fat Diet-Fed Mice.Molecules (Basel, Switzerland) · 2023Article
- Article
- Thyroid hormone responsive protein spot 14 enhances lipogenesis in bovine mammary epithelial cells.In vitro cellular & developmental biology. Animal · 2015Article
- THRSP (thyroid hormone responsive).Atlas of genetics and cytogenetics in oncology and haematology · 2011Article
- Molecular cloning and expression of chicken carbohydrate response element binding protein and Max-like protein X gene homologues.Molecular and cellular biochemistry · 2008Article
- The G115S mutation associated with maturity-onset diabetes of the young impairs hepatocyte nuclear factor 4alpha activities and introduces a PKA phosphorylation site in its DNA-binding domain.The Biochemical journal · 2004Article
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8 authors at 2 institutions in 1 country.
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Abstract
In hepatocytes, the amount of the Spot 14 (S14) protein is closely related to the full expression of enzymes involved in the glycolytic and lipogenic pathways. In the present study we address the role played by this protein in the control of transcription of the L-type pyruvate kinase (L-PK) gene in primary hepatocytes. We show that human S14, which by itself does not bind to the L-PK promoter, physically interacts with the human chicken ovalbumin upstream promoter-transcription factor 1 (COUP-TF1) and induces the switch of this factor from a repressor to an activator. However, the enhancing activity of S14 and COUP-TF1 depends on the presence of a proximal GC-rich box (the L0 element) that specifically binds nuclear proteins from the livers of rats fed a glucose-rich diet. Moreover, the L0 element, which strongly binds dephosphorylated specificity protein 1 (Sp1), loses all affinity when this factor is phosphorylated by cAMP-dependent protein kinase. Mutations that affect binding of Sp1 and nuclear proteins to the L0 box also decrease basal transcription and impair glucose responsiveness of the promoter. These results therefore shed light on the mechanism by which the S14 protein, whose concentration rapidly rises after glucose intake, contributes to the full activity of the L-PK promoter.
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