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Title: The DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification
Authors: Lee, M.B 
Lebedeva, L.A
Suzawa, M
Wadekar, S.A
Desclozeaux, M
Ingraham, H.A
Keywords: cell nucleus receptor
dead box protein dp103
histone deacetylase
liver protein
nuclear receptor DAX 1
receptor activity modifying protein
receptor protein
regulator protein
RNA helicase
steroidogenic factor 1
SUMO protein
unclassified drug
animal cell
cell nucleus inclusion body
controlled study
data analysis
down regulation
enzyme activity
gene expression regulation
mammal cell
mutational analysis
priority journal
protein domain
protein function
protein localization
protein modification
protein phosphorylation
protein processing
regulatory mechanism
transcription regulation
transcription termination
Cell Nucleus
Cercopithecus aethiops
COS Cells
DEAD-box RNA Helicases
DNA-Binding Proteins
Genes, Reporter
Homeodomain Proteins
Intracellular Signaling Peptides and Proteins
Promoter Regions (Genetics)
Protein Inhibitors of Activated STAT
Protein Processing, Post-Translational
Receptors, Cytoplasmic and Nuclear
RNA Helicases
Small Ubiquitin-Related Modifier Proteins
SUMO-1 Protein
Transcription Factors
Transcription, Genetic
Ubiquitin-Protein Ligases
Issue Date: 2005
Citation: Lee, M.B, Lebedeva, L.A, Suzawa, M, Wadekar, S.A, Desclozeaux, M, Ingraham, H.A (2005). The DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification. Molecular and Cellular Biology 25 (5) : 1879-1890. ScholarBank@NUS Repository.
Rights: Attribution 4.0 International
Abstract: Structural analysis of nuclear receptor subfamily V orphan nuclear receptors suggests that ligand-independent mechanisms must regulate this subclass of receptors. Here, we report that steroidogenic factor 1 (SF-1) and liver receptor homolog 1 are repressed via posttranslational SUMO modification at conserved lysines within the hinge domain. Indeed, mutating these lysines or adding the SUMO isopeptidase SENP1 dramatically increased both native and Gal4-chimera receptor activities. The mechanism by which SUMO conjugation attenuates SF-1 activity was found to be largely histone deacetylase independent and was unaffected by the AF2 corepressor Dax1. Instead, our data suggest that SUMO-mediated repression involves direct interaction of the DEAD-box protein DP103 with sumoylated SF-1. Of potential E3-SUMO ligase candidates, PIASy and PIASxα strongly promoted SF-1 sumoylation, and addition of DP103 enhanced both PIAS-dependent receptor sumoylation and SF-1 relocalization to discrete nuclear bodies. Taken together, we propose that DEAD-box RNA helicases are directly coupled to transcriptional repression by protein sumoylation.
Source Title: Molecular and Cellular Biology
ISSN: 02707306
DOI: 10.1128/MCB.25.5.1879-1890.2005
Rights: Attribution 4.0 International
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