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Papers In Press, published online ahead of print October 14, 2003
Cell and Molecular Biology, Catholic University of Chile, Santiago, Metropolitana
Corresponding Author: mandres{at}bio.puc.cl
Nurr1 is a transcription factor essential for the development of ventral dopaminergic neurons. In search for regulatory mechanisms of Nurr1 function, we identified the SUMO-E3 ligase, PIAS
J. Biol. Chem, 10.1074/jbc.M308113200
Submitted on July 25, 2003
Revised on October 9, 2003
Accepted on October 14, 2003
PIAS
represses the transcriptional activation induced by the nuclear receptor Nurr1
, as an interaction partner of Nurr1. Overexpressed PIASand Nurr1 co-localize in the nuclei of transfected cells and their interaction is demonstrated through co-immunoprecipitation and GST pulldown assays. Co-expression of PIAS with Nurr1 results in a potent repression of Nurr1-dependent transcriptional activation of an artificial NBRE reporter as well as of a reporter driven by the native tyrosine hydroxylase promoter. We identified two consensus sumoylation sites in Nurr1. The substitution of lysine 91 by arginine in one SUMO site enhanced the transcriptional activity of Nurr1, while the substitution of lysine 577 by arginine in the second SUMO site decreased transcriptional activity of Nurr1. Interestingly, PIAS-induced repression of Nurr1 activity does not require the two sumoylation sites, since each mutant is repressed as efficiently as the wild type Nurr1. In addition, the mutations do not alter Nurr1 nuclear localization. Finally, we provide evidence that Nurr1 and PIAS co-exist in several nuclei of rodent CNS by demonstrating the co-expression of Nurr1 protein and PIAS mRNA in the same cells. In conclusion, our studies identified PIAS as a transcriptional co-regulator of Nurr1 and suggest that this interaction may have a physiological role in regulating the expression of Nurr1 target genes.
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