PMID- 18250153
OWN - NLM
STAT- MEDLINE
DCOM- 20080421
LR  - 20211020
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 28
IP  - 8
DP  - 2008 Apr
TI  - Acinus-S' represses retinoic acid receptor (RAR)-regulated gene expression 
      through interaction with the B domains of RARs.
PG  - 2549-58
LID - 10.1128/MCB.01199-07 [doi]
AB  - The diverse biological actions of retinoic acid (RA) are mediated by RA receptors 
      (RARs) and retinoid X receptors (RXRs). Modulation of transcription by RARs/RXRs 
      is achieved through two activation functions, ligand-independent AF-1 and 
      ligand-dependent AF-2, located in the A/B and E domains, respectively. While the 
      coregulatory proteins that interact with the E domain are well studied, the A/B 
      domain-interacting partners and their influence(s) on the function of RARs are 
      poorly understood. Acinus-S' is an ubiquitous nuclear protein that has been 
      implicated in inducing apoptotic chromatin condensation and regulating mRNA 
      processing. Our data demonstrate that Acinus-S' can specifically repress 
      ligand-independent and ligand-dependent expression of a DR5 RA response 
      element(RARE)-dependent reporter gene and several endogenous RAR-regulated genes 
      in a dose-dependent and gene-specific manner. Chromatin immunoprecipitation 
      assays show that Acinus-S' associates with RAREs within the promoters of 
      endogenous genes independent of RA treatment. Furthermore, the C-terminal end of 
      Acinus-S' and the B domain of RARbeta interact independently of ligand, and the 
      C-terminal end of Acinus-S' is sufficient for the repression of RAR-regulated 
      gene expression. Finally, histone deacetylase activity only partially accounts 
      for the repressive effect of Acinus-S' on RAR-dependent gene expression. These 
      findings identify Acinus-S' as a novel RAR-interacting protein that regulates the 
      expression of a subset of RAR-regulated genes through direct binding to the 
      N-terminal B domains of RARs.
FAU - Vucetic, Zivjena
AU  - Vucetic Z
AD  - Department of Biochemistry, Temple University School of Medicine, 3440 N. Broad 
      Street, Philadelphia, PA 19140, USA.
FAU - Zhang, Zhenping
AU  - Zhang Z
FAU - Zhao, Jianhua
AU  - Zhao J
FAU - Wang, Fang
AU  - Wang F
FAU - Soprano, Kenneth J
AU  - Soprano KJ
FAU - Soprano, Dianne Robert
AU  - Soprano DR
LA  - eng
GR  - R01 DK044517/DK/NIDDK NIH HHS/United States
GR  - R01 DK067558/DK/NIDDK NIH HHS/United States
GR  - DK67558/DK/NIDDK NIH HHS/United States
GR  - DK44517/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20080204
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (ACIN1 protein, human)
RN  - 0 (Histones)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 9035-51-2 (Cytochrome P-450 Enzyme System)
RN  - EC 1.14.14.1 (Retinoic Acid 4-Hydroxylase)
SB  - IM
MH  - Acetylation
MH  - Amino Acid Motifs
MH  - Animals
MH  - Cell Line
MH  - Conserved Sequence
MH  - Cytochrome P-450 Enzyme System/genetics/metabolism
MH  - *Gene Expression Regulation
MH  - Histones/metabolism
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/genetics/*metabolism
MH  - Promoter Regions, Genetic/genetics
MH  - Protein Binding
MH  - Receptors, Retinoic Acid/chemistry/genetics/*metabolism
MH  - Retinoic Acid 4-Hydroxylase
PMC - PMC2293115
EDAT- 2008/02/06 09:00
MHDA- 2008/04/22 09:00
PMCR- 2008/08/01
CRDT- 2008/02/06 09:00
PHST- 2008/02/06 09:00 [pubmed]
PHST- 2008/04/22 09:00 [medline]
PHST- 2008/02/06 09:00 [entrez]
PHST- 2008/08/01 00:00 [pmc-release]
AID - MCB.01199-07 [pii]
AID - 1199-07 [pii]
AID - 10.1128/MCB.01199-07 [doi]
PST - ppublish
SO  - Mol Cell Biol. 2008 Apr;28(8):2549-58. doi: 10.1128/MCB.01199-07. Epub 2008 Feb 
      4.