scholarly journals IFL1, a Gene Regulating Interfascicular Fiber Differentiation in Arabidopsis, Encodes a Homeodomain-Leucine Zipper Protein

1999 ◽  
Vol 11 (11) ◽  
pp. 2139-2152 ◽  
Author(s):  
Ruiqin Zhong ◽  
Zheng-Hua Ye



1994 ◽  
Vol 269 (2) ◽  
pp. 1091-1098
Author(s):  
F.C. Bange ◽  
U. Vogel ◽  
T. Flohr ◽  
M. Kiekenbeck ◽  
B. Denecke ◽  
...  


Author(s):  
Minsoo Kang ◽  
Sun Kyoung Han ◽  
Suhyun Kim ◽  
Sungyeon Park ◽  
Yerin Jo ◽  
...  

Abstract Hepatic gluconeogenesis is the central pathway for glucose generation in the body. The imbalance between glucose synthesis and uptake leads to metabolic diseases such as obesity, diabetes, and cardiovascular diseases. Small leucine zipper protein (sLZIP) is an isoform of LZIP and it mainly functions as a transcription factor. Although sLZIP is known to regulate the transcription of genes involved in various cellular processes, the role of sLZIP in hepatic glucose metabolism is not known. In this study, we investigated the regulatory role of sLZIP in hepatic gluconeogenesis and its involvement in metabolic disorder. We found that sLZIP expression was elevated during glucose starvation, leading to the promotion of phosphoenolpyruvate carboxylase and glucose-6-phosphatase expression in hepatocytes. However, sLZIP knockdown suppressed the expression of the gluconeogenic enzymes under low glucose conditions. sLZIP also enhanced glucose production in the human liver cells and mouse primary hepatic cells. Fasting-induced cyclic adenosine monophosphate impeded sLZIP degradation. Results of glucose and pyruvate tolerance tests showed that sLZIP transgenic mice exhibited abnormal blood glucose metabolism. These findings suggest that sLZIP is a novel regulator of gluconeogenic enzyme expression and plays a role in blood glucose homeostasis during starvation.



1995 ◽  
Vol 15 (1) ◽  
pp. 208-216 ◽  
Author(s):  
L Kuras ◽  
D Thomas

Transcription of the genes necessary for sulfur amino acid biosynthesis in Saccharomyces cerevisiae is dependent on Met4, a transcriptional activator that belongs to the basic region-leucine zipper protein family. In this report, we show that one mechanism permitting the repression of the sulfur network by S-adenosylmethionine (AdoMet) involves inhibition of the transcriptional activation function of Met4. Using a wide array of deleted LexA-Met4 fusion proteins as well as various Gal4-Met4 hybrids, we identify the functional domains of Met4 and characterize their relationship. Met4 appears to contain only one activation domain, located in its N-terminal part. We demonstrate that this activation domain functions in a constitutive manner and that AdoMet responsiveness requires a distinct region of Met4. Furthermore, we show that when fused to a heterologous activation domain, this inhibitory region confers inhibition by AdoMet. Met4 contains another distinct functional domain that appears to function as an antagonist of the inhibitory region when intracellular AdoMet is low. On the basis of the presented results, a model for intramolecular regulation of Met4 is proposed.



2018 ◽  
Vol 46 (20) ◽  
pp. 11030-11047 ◽  
Author(s):  
C Joaquín Cáceres ◽  
Jenniffer Angulo ◽  
Fernando Lowy ◽  
Nataly Contreras ◽  
Beth Walters ◽  
...  


Plant Science ◽  
2021 ◽  
pp. 111159
Author(s):  
Peng Jiao ◽  
Zhenzhong Jiang ◽  
Xiaotong Wei ◽  
Siyan Liu ◽  
Jing Qu ◽  
...  








Biochemistry ◽  
2004 ◽  
Vol 43 (50) ◽  
pp. 15845-15851 ◽  
Author(s):  
Adriana E. Tron ◽  
Elina Welchen ◽  
Daniel H. Gonzalez


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