scholarly journals Retraction Notice to: The Chromatin-Remodeling Complex WINAC Targets a Nuclear Receptor to Promoters and Is Impaired in Williams Syndrome

Cell ◽  
2012 ◽  
Vol 149 (1) ◽  
pp. 245
Author(s):  
Hirochika Kitagawa ◽  
Ryoji Fujiki ◽  
Kimihiro Yoshimura ◽  
Yoshihiro Mezaki ◽  
Yoshikatsu Uematsu ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Chromatin Remodeling ◽  
Williams Syndrome ◽  
Chromatin Remodeling Complex ◽  
Retraction Notice

scholarly journals RETRACTED: The Chromatin-Remodeling Complex WINAC Targets a Nuclear Receptor to Promoters and Is Impaired in Williams Syndrome

Cell ◽  
2003 ◽  
Vol 113 (7) ◽  
pp. 905-917 ◽  
Author(s):  
Hirochika Kitagawa ◽  
Ryoji Fujiki ◽  
Kimihiro Yoshimura ◽  
Yoshihiro Mezaki ◽  
Yoshikatsu Uematsu ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Chromatin Remodeling ◽  
Williams Syndrome ◽  
Chromatin Remodeling Complex

Nuclear receptor coactivators: the key to unlock chromatin

2005 ◽  
Vol 83 (4) ◽  
pp. 418-428 ◽  
Author(s):  
Wei Xu
Keyword(s):  
Nuclear Receptors ◽  
Nuclear Receptor ◽  
Chromatin Remodeling ◽  
Transcriptional Activation ◽  
Transcriptional Control ◽  
Biological Effects ◽  
Gene Activation ◽  
Nuclear Hormone Receptor ◽  
Nuclear Receptor Coactivators ◽  
Chromatin Remodeling Complex

The biological effects of hormones, ranging from organogenesis, metabolism, and proliferation, are transduced through nuclear receptors (NRs). Over the last decade, NRs have been used as a model to study transcriptional control. The conformation of activated NRs is favorable for the recruitment of coactivators, which promote transcriptional activation by directly communicating with chromatin. This review will focus on the function of different classes of coactivators and associated complexes, and on progress in our understanding of gene activation by NRs through chromatin remodeling.Key words: nuclear hormone receptor, p160 family of coactivators, histone modification, chromatin remodeling complex.

scholarly journals Crucial Roles for Interactions between MLL3/4 and INI1 in Nuclear Receptor Transactivation

2009 ◽  
Vol 23 (5) ◽  
pp. 610-619 ◽  
Author(s):  
Seunghee Lee ◽  
Dae-Hwan Kim ◽  
Young Hwa Goo ◽  
Young Chul Lee ◽  
Soo-Kyung Lee ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Chromatin Remodeling ◽  
Target Genes ◽  
Mutational Analysis ◽  
Specific Protein ◽  
Transcriptional Coactivator ◽  
Set Domain ◽  
Protein Protein Interaction ◽  
Terminal Set ◽  
Chromatin Remodeling Complex

Abstract Nuclear receptor (NR) transactivation involves multiple coactivators, and the molecular basis for how these are functionally integrated needs to be determined to fully understand the NR action. Activating signal cointegrator-2 (ASC-2), a transcriptional coactivator of many NRs and transcription factors, forms a steady-state complex, ASCOM (for ASC-2 complex), which contains histone H3-lysine-4 (H3K4) methyltransferase MLL3 or its paralog MLL4. Here, we show that ASCOM requires a functional cross talk with the ATPase-dependent chromatin remodeling complex Swi/Snf for efficient NR transactivation. Our results reveal that ASCOM and Swi/Snf are tightly colocalized in the nucleus and that ASCOM and Swi/Snf promote each other’s binding to NR target genes. We further show that the C-terminal SET domain of MLL3 and MLL4 directly interacts with INI1, an integral subunit of Swi/Snf. Our mutational analysis demonstrates that this interaction underlies the mutual facilitation of ASCOM and Swi/Snf recruitment to NR target genes. Importantly, this study uncovers a specific protein-protein interaction as a novel venue to couple two distinct enzymatic coactivator complexes during NR transactivation.

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