scholarly journals The Orphan Nuclear Receptor TR2 Interacts Directly with Both Class I and Class II Histone Deacetylases

2001 ◽  
Vol 15 (8) ◽  
pp. 1318-1328 ◽  
Author(s):  
Peter J. Franco ◽  
Mariya Farooqui ◽  
Edward Seto ◽  
Li-Na Wei
Keyword(s):  
Nuclear Receptor ◽  
Histone Deacetylases ◽  
Class Ii ◽  
Class I ◽  
Orphan Nuclear Receptor

scholarly journals Functional Interaction between Class II Histone Deacetylases and ICP0 of Herpes Simplex Virus Type 1

2004 ◽  
Vol 78 (13) ◽  
pp. 6744-6757 ◽  
Author(s):  
Patrick Lomonte ◽  
Joëlle Thomas ◽  
Pascale Texier ◽  
Cécile Caron ◽  
Saadi Khochbin ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Histone Deacetylases ◽  
Class Ii ◽  
Class I ◽  
Transfected Cells ◽  
Amino Terminal ◽  
Simplex Virus ◽  
Class I Hdacs

ABSTRACT This study describes the physical and functional interactions between ICP0 of herpes simplex virus type 1 and class II histone deacetylases (HDACs) 4, 5, and 7. Class II HDACs are mainly known for their participation in the control of cell differentiation through the regulation of the activity of the transcription factor MEF2 (myocyte enhancer factor 2), implicated in muscle development and neuronal survival. Immunofluorescence experiments performed on transfected cells showed that ICP0 colocalizes with and reorganizes the nuclear distribution of ectopically expressed class I and II HDACs. In addition, endogenous HDAC4 and at least one of its binding partners, the corepressor protein SMRT (for silencing mediator of retinoid and thyroid receptor), undergo changes in their nuclear distribution in ICP0-transfected cells. As a result, during infection endogenous HDAC4 colocalizes with ICP0. Coimmunoprecipitation and glutathione S-transferase pull-down assays confirmed that class II but not class I HDACs specifically interacted with ICP0 through their amino-terminal regions. This region, which is not conserved in class I HDACs but homologous to the MITR (MEF2-interacting transcription repressor) protein, is responsible for the repression, in a deacetylase-independent manner, of MEF2 by sequestering it under an inactive form in the nucleus. Consequently, we show that ICP0 is able to overcome the HDAC5 amino-terminal- and MITR-induced MEF2A repression in gene reporter assays. This is the first report of a viral protein interacting with and controlling the repressor activity of class II HDACs. We discuss the putative consequences of such an interaction for the biology of the virus both during lytic infection and reactivation from latency.

Inhibitors of histone deacetylases in class I and class II suppress human osteoclasts in vitro

2011 ◽  
Vol 226 (12) ◽  
pp. 3233-3241 ◽  
Author(s):  
M.D. Cantley ◽  
D.P. Fairlie ◽  
P.M. Bartold ◽  
K.D. Rainsford ◽  
G.T. Le ◽  
...  
Keyword(s):  
Histone Deacetylases ◽  
Class Ii ◽  
Class I ◽  
Human Osteoclasts

scholarly journals Class I and Class II Histone Deacetylases Are Potential Therapeutic Targets for Treating Pancreatic Cancer

PLoS ONE ◽  
2012 ◽  
Vol 7 (12) ◽  
pp. e52095 ◽  
Author(s):  
Guan Wang ◽  
Jing He ◽  
Jianyun Zhao ◽  
Wenting Yun ◽  
Chengzhi Xie ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Histone Deacetylases ◽  
Therapeutic Targets ◽  
Class Ii ◽  
Class I

scholarly journals Inhibition of Polyomavirus ori-Dependent DNA Replication by mSin3B

2002 ◽  
Vol 76 (23) ◽  
pp. 11809-11818 ◽  
Author(s):  
An-Yong Xie ◽  
William R. Folk
Keyword(s):  
Dna Replication ◽  
Histone Deacetylases ◽  
Trichostatin A ◽  
Class Ii ◽  
T Antigen ◽  
Class I ◽  
Large T Antigen ◽  
Transcriptional Corepressor ◽  
Independent Mechanism

ABSTRACT When tethered in cis to DNA, the transcriptional corepressor mSin3B inhibits polyomavirus (Py) ori-dependent DNA replication in vivo. Histone deacetylases (HDACs) appear not to be involved, since tethering class I and class II HDACs in cis does not inhibit replication and treating the cells with trichostatin A does not specifically relieve inhibition by mSin3B. However, the mSin3B L59P mutation that impairs mSin3B interaction with N-CoR/SMRT abrogates inhibition of replication, suggesting the involvement of N-CoR/SMRT. Py large T antigen interacts with mSin3B, suggesting an HDAC-independent mechanism by which mSin3B inhibits DNA replication.

scholarly journals HDACs class II-selective inhibition alters nuclear receptor-dependent differentiation

2010 ◽  
Vol 45 (4) ◽  
pp. 219-228 ◽  
Author(s):  
Angela Nebbioso ◽  
Carmela Dell'Aversana ◽  
Anne Bugge ◽  
Roberta Sarno ◽  
Sergio Valente ◽  
...  
Keyword(s):  
Histone Deacetylases ◽  
Selective Inhibition ◽  
Class Ii ◽  
Class I ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
F9 Cells ◽  
Anti Cancer ◽  
Cardiovascular Defects

Epigenetic deregulation contributes to diseases including cancer, neurodegeneration, osteodystrophy, cardiovascular defects, and obesity. For this reason, several inhibitors for histone deacetylases (HDACs) are being validated as novel anti-cancer drugs in clinical studies and display important anti-proliferative activities. While most inhibitors act on both class I, II, and IV HDACs, evidence is accumulating that class I is directly involved in regulation of cell growth and death, whereas class II members regulate differentiation processes, such as muscle and neuronal differentiation. Here, we show that the novel class II-selective inhibitor MC1568 interferes with the RAR- and peroxisome proliferator-activated receptor γ (PPARγ)-mediated differentiation-inducing signaling pathways. In F9 cells, this inhibitor specifically blocks endodermal differentiation despite not affecting retinoic acid-induced maturation of promyelocytic NB4 cells. In 3T3-L1 cells, MC1568 attenuates PPARγ-induced adipogenesis, while the class I-selective MS275 blocked adipogenesis completely thus revealing a different mode of action and/or target profile of the two classes of HDACs. Using in vivo reporting PPRE-Luc mice, we find that MC1568 impairs PPARγ signaling mostly in the heart and adipose tissues. These results illustrate how HDAC functions can be dissected by selective inhibitors.

scholarly journals Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression

2000 ◽  
Vol 14 (1) ◽  
pp. 55-66 ◽  
Author(s):  
Hung-Ying Kao ◽  
Michael Downes ◽  
Peter Ordentlich ◽  
Ronald M. Evans
Keyword(s):  
Histone Deacetylase ◽  
Histone Deacetylases ◽  
Mammalian Cells ◽  
Class Ii ◽  
Class I ◽  
Nuclear Compartment ◽  
New Family ◽  
Repressive Effect ◽  
Two Hybrid

The transcriptional corepressor SMRT functions by mediating the repressive effect of transcription factors involved in diverse signaling pathways. The mechanism by which SMRT represses basal transcription has been proposed to involve the indirect recruitment of histone deacetylase HDAC1 via the adaptor mSin3A. In contrast to this model, a two-hybrid screen on SMRT-interacting proteins resulted in the isolation of the recently described HDAC5 and a new family member termed HDAC7. Molecular and biochemical results indicate that this interaction is direct and in vivo evidence colocalizes SMRT, mHDAC5, and mHDAC7 to a distinct nuclear compartment. Surprisingly, HDAC7 can interact with mSin3A in yeast and in mammalian cells, suggesting association of multiple repression complexes. Taken together, our results provide the first evidence that SMRT-mediated repression is promoted by class I and class II histone deacetylases and that SMRT can recruit class II histone deacetylases in a mSin3A-independent fashion.

Sign in / Sign up

Export Citation Format

Share Document