scholarly journals LSD1 Regulates Pluripotency of Embryonic Stem/Carcinoma Cells through Histone Deacetylase 1-Mediated Deacetylation of Histone H4 at Lysine 16

2013 ◽  
Vol 34 (2) ◽  
pp. 158-179 ◽  
Author(s):  
F. Yin ◽  
R. Lan ◽  
X. Zhang ◽  
L. Zhu ◽  
F. Chen ◽  
...  
2021 ◽  
Author(s):  
Claire Barnes ◽  
David English ◽  
Megan Broderick ◽  
Mark Collins ◽  
Shaun M Cowley

Lysine specific demethylase 1 (LSD1) regulates gene expression as part of the CoREST complex, along with co-repressor of REST (CoREST) and histone deacetylase 1 (HDAC1). CoREST is recruited to specific...


Apmis ◽  
2008 ◽  
Vol 116 (5) ◽  
pp. 420-421
Author(s):  
Lena Marquard ◽  
Christian Bjørn Poulsen ◽  
Ib Jarle Christensen ◽  
Peter Buhl Ralfkiær ◽  
Maxwell Sehested

2009 ◽  
Vol 54 (6) ◽  
pp. 688-698 ◽  
Author(s):  
Lena Marquard ◽  
Christian B Poulsen ◽  
Lise Mette Gjerdrum ◽  
Peter de Nully Brown ◽  
Ib J Christensen ◽  
...  

2007 ◽  
Vol 27 (10) ◽  
pp. 3578-3588 ◽  
Author(s):  
Bong Gu Kang ◽  
June Ho Shin ◽  
Jae Kyu Yi ◽  
Ho Chul Kang ◽  
Jong Joo Lee ◽  
...  

ABSTRACT A transcription corepressor, MAT1-mediated transcriptional repressor (MMTR), was found in mouse embryonic stem cell lines. MMTR orthologs (DMAP1) are found in a wide variety of life forms from yeasts to humans. MMTR down-regulation in differentiating mouse embryonic stem cells in vitro resulted in activation of many unrelated genes, suggesting its role as a general transcriptional repressor. In luciferase reporter assays, the transcriptional repression activity resided at amino acids 221 to 468. Histone deacetylase 1 (HDAC1) interacts with MMTR both in vitro and in vivo and also interacts with MMTR in the nucleus. Interestingly, MMTR activity was only partially rescued by competition with dominant-negative HDAC1(H141A) or by treatment with an HDAC inhibitor, trichostatin A (TSA). To identify the protein responsible for HDAC1-independent MMTR activity, we performed a yeast two-hybrid screen with the full-length MMTR coding sequence as bait and found MAT1. MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase which constitutes a subcomplex of TFIIH. The coiled-coil domain in the middle of MAT1 was confirmed to interact with the C-terminal half of MMTR, and the MMTR-mediated transcriptional repression activity was completely restored by MAT1 in the presence of TSA. Moreover, intact MMTR was required to inhibit phosphorylation of the C-terminal domain in the RNA polymerase II largest subunit by TFIIH kinase in vitro. Taken together, these data strongly suggest that MMTR is part of the basic cellular machinery for a wide range of transcriptional regulation via interaction with TFIIH and HDAC.


2016 ◽  
Vol 292 (6) ◽  
pp. 2422-2440 ◽  
Author(s):  
Renata C. Ferreira ◽  
Evgenya Y. Popova ◽  
Jessica James ◽  
Marcelo R. S. Briones ◽  
Samuel S. Zhang ◽  
...  

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