Nuclear S6K1 regulates cAMP-responsive element-dependent gene transcription through activation of mTOR signal pathway

Author(s):  
Ye Ji Jeon ◽  
Sang Ah Yi ◽  
Jaecheol Lee ◽  
Jeung-Whan Han
2000 ◽  
Vol 164 (3) ◽  
pp. R11-R16 ◽  
Author(s):  
A Takenaka ◽  
K Komori ◽  
T Morishita ◽  
SI Takahashi ◽  
T Hidaka ◽  
...  

To investigate the molecular mechanisms of increased transcription of the insulin-like growth factor-binding protein-1 (IGFBP-1) gene in dietary protein-deprived animals, the cis-acting sequence that is involved in this regulation was analyzed. We first showed that IGFBP-1 gene transcription was up-regulated by amino acid deprivation in cultured liver cell lines: H4IIE and HuH-7. Since HuH-7 cells showed a greater increase in IGFBP-1 mRNA in response to amino acid deprivation, this cell line was used in further experiments. Using a promoter function assay, we found that up-regulation of promoter activity responding to amino acid deprivation was abolished by deleting the region between -112 and -81 bp from the cap site from the gene construct. This cis-acting region includes the insulin-responsive element (IRE) and glucocorticoid responsive element (GRE) of IGFBP-1. In summary, the present observation suggests that the 32-bp (-112 to -81) in the IGFBP-1 gene 5' promoter region is involved in the induction of the IGFBP-1 gene in response to amino acid deprivation.


1991 ◽  
Vol 11 (5) ◽  
pp. 2826-2831
Author(s):  
M A Collart ◽  
N Tourkine ◽  
D Belin ◽  
P Vassalli ◽  
P Jeanteur ◽  
...  

Cultured mouse thioglycolate-elicited peritoneal macrophages exhibit a strong block to transcriptional elongation beyond the end of the c-fos gene first exon. This block is absent in freshly isolated peritoneal cells, appears slowly during culture, and does not require adherence of the cells. The extent of this block is largely responsible for the levels of c-fos mRNA in cultured macrophages, even after modulation by agents such as the tumor promoter phorbol myristate acetate and increased intracellular cyclic AMP, which also increase the activity of the c-fos promoter. When macrophages are cultured in the absence of mobilizable calcium, the block can no longer be relieved by any inducing agent. Conversely, upon calcium influxes, there is little alteration in the level of transcriptional initiation, but transcription proceeds efficiently through the entire c-fos locus. These results suggest the presence of an intragenic calcium-responsive element in the c-fos gene and illustrate its key role in the control of c-fos gene transcription.


2002 ◽  
Vol 357 (1423) ◽  
pp. 877-886 ◽  
Author(s):  
C. Viswanathan ◽  
Jian-Kang Zhu

Chilling and freezing temperatures adversely affect the productivity and quality of crops. Hence improving the cold hardiness of crop plants is an important goal in agriculture, which demands a clear understanding of cold stress signal perception and transduction. Pharmacological and biochemical evidence shows that membrane rigidification followed by cytoskeleton rearrangement, Ca 2+ influx and Ca 2+ –dependent phosphorylation are involved in cold stress signal transduction. Cold–responsive genes are regulated through C–repeat/dehydration–responsive elements (CRT/DRE) and abscisic acid (ABA)–responsive element cis elements by transacting factors C–repeat binding factors/dehydration–responsive element binding proteins (CBFs/DREBs) and basic leucine zippers (bZIPs) (SGBF1), respectively. We have carried out a forward genetic analysis using chemically mutagenized Arabidopsis plants expressing cold–responsive RD29A promoter–driven luciferase to dissect cold signal transduction. We have isolated the fiery1 ( fry1 ) mutant and cloned the FRY1 gene, which encodes an inositol polyphosphate 1–phosphatase. The fry1 plants showed enhanced induction of stress genes in response to cold, ABA, salt and dehydration due to higher accumulation of the second messenger, inositol (1,4,5)– triphosphate (IP 3 ). Thus our study provides genetic evidence suggesting that cold signal is transduced through changes in IP 3 levels. We have also identified the hos1 mutation, which showed super induction of cold–responsive genes and their transcriptional activators. Molecular cloning and characterization revealed that HOS1 encodes a ring finger protein, which has been implicated as an E3 ubiquitin conjugating enzyme. HOS1 is present in the cytoplasm at normal growth temperatures but accumulates in the nucleus upon cold stress. HOS1 appears to regulate temperature sensing by the cell as cold–responsive gene expression occurs in the hos1 mutant at relatively warm temperatures. Thus HOS1 is a negative regulator, which may be functionally linked to cellular thermosensors to modulate cold–responsive gene transcription.


Placenta ◽  
2007 ◽  
Vol 28 (8-9) ◽  
pp. 898-906 ◽  
Author(s):  
F. López-Díaz ◽  
R. Nores ◽  
G. Panzetta-Dutari ◽  
D. Slavin ◽  
C. Prieto ◽  
...  

2001 ◽  
Vol 29 (2) ◽  
pp. 310-316 ◽  
Author(s):  
J.-F. Louet ◽  
C. Le May ◽  
J.-P. Pégorier ◽  
J.-F. Decaux ◽  
J. Girard

This brief review focuses on the transcriptional regulation of liver carnitine palmitoyltransferase I (L-CPT I) by pancreatic and thyroid hormones and by long-chain fatty acids (LCFA). Both glucagon and 3,3′,5-tri-iodothyronine (T3) enhanced the transcription of the gene encoding L-CPT I, whereas insulin had the opposite effect. Interestingly, the transcriptional effect of T3 required, in addition to the thyroid-responsive element, the co-operation of a sequence located in the first intron of L-CPT I gene. Non-esterified fatty acids rather than acyl-CoA ester or intramitochondrial metabolite were responsible for the transcriptional effect on the gene encoding LCPT I. It was shown that LCFA and peroxisome proliferators stimulated L-CPT I gene transcription by distinct mechanisms. Peroxisome proliferator stimulated L-CPT I gene transcription through a peroxisome-proliferator-responsive element (PPRE) located at -2846 bp, whereas LCFA induced L-CPT I gene transcription through a peroxisome-proliferator-activated receptor α (PPARα)-independent mechanism owing to a sequence located in the first intron of the gene.


2010 ◽  
Vol 21 (8) ◽  
pp. 757-763 ◽  
Author(s):  
Saskia T.J. van Cruchten ◽  
Laura H.J. de Haan ◽  
Patrick P.J. Mulder ◽  
Cindy Kunne ◽  
Mark V. Boekschoten ◽  
...  

1991 ◽  
Vol 11 (5) ◽  
pp. 2826-2831 ◽  
Author(s):  
M A Collart ◽  
N Tourkine ◽  
D Belin ◽  
P Vassalli ◽  
P Jeanteur ◽  
...  

Cultured mouse thioglycolate-elicited peritoneal macrophages exhibit a strong block to transcriptional elongation beyond the end of the c-fos gene first exon. This block is absent in freshly isolated peritoneal cells, appears slowly during culture, and does not require adherence of the cells. The extent of this block is largely responsible for the levels of c-fos mRNA in cultured macrophages, even after modulation by agents such as the tumor promoter phorbol myristate acetate and increased intracellular cyclic AMP, which also increase the activity of the c-fos promoter. When macrophages are cultured in the absence of mobilizable calcium, the block can no longer be relieved by any inducing agent. Conversely, upon calcium influxes, there is little alteration in the level of transcriptional initiation, but transcription proceeds efficiently through the entire c-fos locus. These results suggest the presence of an intragenic calcium-responsive element in the c-fos gene and illustrate its key role in the control of c-fos gene transcription.


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