scholarly journals Sequential activation of transcription factors in lens induction

2000 ◽  
Vol 42 (5) ◽  
pp. 437-448 ◽  
Author(s):  
Hajime Ogino ◽  
Kunio Yasuda
2007 ◽  
Vol 72 (5) ◽  
pp. 552-557 ◽  
Author(s):  
N. A. Bolotina ◽  
A. V. Gasparian ◽  
T. K. Dubovaja ◽  
V. A. Evteev ◽  
V. A. Kobliakov

2018 ◽  
Vol 19 (10) ◽  
pp. 3284 ◽  
Author(s):  
Brijesh Kumar Singh ◽  
Rohit Anthony Sinha ◽  
Paul Michael Yen

The thyroid hormone plays a key role in energy and nutrient metabolisms in many tissues and regulates the transcription of key genes in metabolic pathways. It has long been believed that thyroid hormones (THs) exerted their effects primarily by binding to nuclear TH receptors (THRs) that are associated with conserved thyroid hormone response elements (TREs) located on the promoters of target genes. However, recent transcriptome and ChIP-Seq studies have challenged this conventional view as discordance was observed between TH-responsive genes and THR binding to DNA. While THR association with other transcription factors bound to DNA, TH activation of THRs to mediate effects that do not involve DNA-binding, or TH binding to proteins other than THRs have been invoked as potential mechanisms to explain this discrepancy, it appears that additional novel mechanisms may enable TH to regulate the mRNA expression. These include activation of transcription factors by SIRT1 via metabolic actions by TH, the post-translational modification of THR, the THR co-regulation of transcription with other nuclear receptors and transcription factors, and the microRNA (miR) control of RNA transcript expression to encode proteins involved in the cellular metabolism. Together, these novel mechanisms enlarge and diversify the panoply of metabolic genes that can be regulated by TH.


2000 ◽  
Vol 59 (8) ◽  
pp. 997-1005 ◽  
Author(s):  
Alvaro Puga ◽  
Sonya J Barnes ◽  
Ching-yi Chang ◽  
Huan Zhu ◽  
Kenneth P Nephew ◽  
...  

1996 ◽  
Vol 76 (3) ◽  
pp. 839-885 ◽  
Author(s):  
H. F. Bunn ◽  
R. O. Poyton

This review focuses on the molecular stratagems utilized by bacteria, yeast, and mammals in their adaptation to hypoxia. Among this broad range of organisms, changes in oxygen tension appear to be sensed by heme proteins, with subsequent transfer of electrons along a signal transduction pathway which may depend on reactive oxygen species. These heme-based sensors are generally two-domain proteins. Some are hemokinases, while others are flavohemoproteins [flavohemoglobins and NAD(P)H oxidases]. Hypoxia-dependent kinase activation of transcription factors in nitrogen-fixing bacteria bears a striking analogy to the phosphorylation of hypoxia inducible factor-1 (HIF-1) in mammalian cells. Moreover, redox chemistry appears to play a critical role both in the trans-activation of oxygen-responsive genes in unicellular organisms as well as in the activation of HIF-1. In yeast and bacteria, regulatory operons coordinate expression of genes responsible for adaptive responses to hypoxia and hyperoxia. Similarly, in mammals, combinatorial interactions of HIF-1 with other identified transcription factors are required for the hypoxic induction of physiologically important genes.


Nature ◽  
1997 ◽  
Vol 386 (6627) ◽  
pp. 855-858 ◽  
Author(s):  
Ricardo E. Dolmetsch ◽  
Richard S. Lewis ◽  
Christopher C. Goodnow ◽  
James I. Healy

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