Abstract
SUMOylation regulates a variety of cellular processes, including control of transcriptional activities of nuclear receptors. Here, we present SUMOylation of orphan nuclear receptor, RORalpha by both SUMO-1 and SUMO-2. SUMOylation of RORalpha occurred on the 240th lysine residue at the hinge region of human protein. PIAS family members, PIASxalpha, PIAS3, and PIASy, increased SUMOylation of RORalpha, whereas SENP2 specifically removed SUMO from RORalpha. SUMOylation-defective mutant form of RORalpha exhibited decreased transcriptional activity on RORalpha-responsive promoters indicating that SUMOylation may positively regulate transcriptional function of RORalpha.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Cysteine Endopeptidases / metabolism
-
HeLa Cells
-
Humans
-
Mutation
-
Nuclear Receptor Subfamily 1, Group F, Member 1
-
Promoter Regions, Genetic
-
Protein Inhibitors of Activated STAT / metabolism
-
Receptors, Cytoplasmic and Nuclear / genetics
-
Receptors, Cytoplasmic and Nuclear / metabolism*
-
SUMO-1 Protein / genetics
-
SUMO-1 Protein / metabolism*
-
Small Ubiquitin-Related Modifier Proteins / genetics
-
Small Ubiquitin-Related Modifier Proteins / metabolism*
-
Trans-Activators / genetics
-
Trans-Activators / metabolism*
-
Transcriptional Activation*
Substances
-
Nuclear Receptor Subfamily 1, Group F, Member 1
-
Protein Inhibitors of Activated STAT
-
RORA protein, human
-
Receptors, Cytoplasmic and Nuclear
-
SUMO-1 Protein
-
SUMO1 protein, human
-
SUMO2 protein, human
-
Small Ubiquitin-Related Modifier Proteins
-
Trans-Activators
-
Cysteine Endopeptidases
-
SENP2 protein, human