scholarly journals Myocyte enhancer factor‐2 and p300 interact to regulate the expression of homeostatic regulator Pumilio in Drosophila

Author(s):  
Wei‐Hsiang Lin ◽  
Richard A. Baines
2004 ◽  
Vol 127 (4) ◽  
pp. 1174-1188 ◽  
Author(s):  
Xuemin Wang ◽  
Xiaoli Tang ◽  
Xiaoming Gong ◽  
Efsevia Albanis ◽  
Scott L. Friedman ◽  
...  

2008 ◽  
Vol 284 (9) ◽  
pp. 5592-5601 ◽  
Author(s):  
Keisuke Sako ◽  
Shigetomo Fukuhara ◽  
Takashi Minami ◽  
Takao Hamakubo ◽  
Haihua Song ◽  
...  

2010 ◽  
Vol 106 (1) ◽  
pp. 155-165 ◽  
Author(s):  
Eva van Rooij ◽  
Jens Fielitz ◽  
Lillian B. Sutherland ◽  
Victor L. Thijssen ◽  
Harry J. Crijns ◽  
...  

Genetics ◽  
2005 ◽  
Vol 170 (4) ◽  
pp. 1747-1759 ◽  
Author(s):  
Phillip W. Baker ◽  
Kathleen K. Kelly Tanaka ◽  
Niels Klitgord ◽  
Richard M. Cripps

Circulation ◽  
2015 ◽  
Vol 131 (2) ◽  
pp. 190-199 ◽  
Author(s):  
Jongmin Kim ◽  
Cheol Hwangbo ◽  
Xiaoyue Hu ◽  
Yujung Kang ◽  
Irinna Papangeli ◽  
...  

2009 ◽  
Vol 29 (12) ◽  
pp. 3355-3366 ◽  
Author(s):  
R. L. S. Perry ◽  
C. Yang ◽  
N. Soora ◽  
J. Salma ◽  
M. Marback ◽  
...  

ABSTRACT The myocyte enhancer factor 2 (MEF2) transcription factors play important roles in neuronal, cardiac, and skeletal muscle tissues. MEF2 serves as a nuclear sensor, integrating signals from several signaling cascades through protein-protein interactions with kinases, chromatin remodeling factors, and other transcriptional regulators. Here, we report a novel interaction between the catalytic subunit of protein phosphatase 1α (PP1α) and MEF2. Interaction occurs within the nucleus, and binding of PP1α to MEF2 potently represses MEF2-dependent transcription. The interaction utilizes uncharacterized domains in both PP1α and MEF2, and PP1α phosphatase activity is not obligatory for MEF2 repression. Moreover, a MEF2-PP1α regulatory complex leads to nuclear retention and recruitment of histone deacetylase 4 to MEF2 transcription complexes. PP1α-mediated repression of MEF2 overrides the positive influence of calcineurin signaling, suggesting PP1α exerts a dominant level of control over MEF2 function. Indeed, PP1α-mediated repression of MEF2 function interferes with the prosurvival effect of MEF2 in primary hippocampal neurons. The PP1α-MEF2 interaction constitutes a potent locus of control for MEF2-dependent gene expression, having potentially important implications for neuronal cell survival, cardiac remodeling in disease, and terminal differentiation of vascular, cardiac, and skeletal muscle.


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