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Am J Physiol Endocrinol Metab (December 17, 2002). doi:10.1152/ajpendo.00390.2002
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Articles in PresS, published online ahead of print December 17, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00390.2002
Submitted on September 3, 2002
Accepted on December 8, 2002

Sumoylation of Pdx1 Is Associated with Its Nuclear Localization and Insulin Gene Activation

Akio Kishi1, Takaaki Nakamura2, Yoshihiko Nishio1, Hiroshi Maegawa1, and Atsunori Kashiwagi1*

1 Division of Endocrinology and Metabolism, Department of Medicine, Shiga University of Medical Science, Otsu, Shiga, Japan
2 Department of Anatomy, Shiga University of Medical Science, Otsu, Shiga, Japan

* To whom correspondence should be addressed. E-mail: kasiwagi{at}belle.shiga-med.ac.jp.

Pancreatic duodenal homeobox-1 (Pdx1) is a transcription factor and its phosphorylation is thought to be essential for activation of insulin gene expression. This phosphorylation is related to a concomitant shift in molecular mass from 31 to 46 kDa. However, we found that Pdx1 was modified by SUMO-1 (small ubiquitin-related modifier 1) in {beta}-TC-6 as well as COS-7 cells, which were transfected with Pdx1 cDNA. This modification contributed to the increase in molecular mass of Pdx1 from 31 to 46 kDa. Additionally, sumoylated Pdx1 localized in the nucleus. The reduction of SUMO-1 protein using RNA interference (SUMO-iRNAs) resulted in a significant decrease in Pdx1 protein in the nucleus. A 34 kDa form of Pdx1 was detected by the cells exposed to SUMO-iRNAs in the presence of lactacystin, a proteasome inhibitor. Furthermore, the reduced nuclear sumoylated Pdx1 content was associated with significant lower transcriptional activity of insulin gene. These findings indicate that SUMO-1 modification is associated with both the localization and stability of Pdx1 as well as its effect on insulin gene activation.




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