SUMO modification regulates the transcriptional repressor function of aryl hydrocarbon receptor repressor

Motohiko Oshima, Junsei Mimura, Hiroki Sekine, Hiromi Okawa, Yoshiaki Fujii-Kuriyama

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)

Abstract

The aryl hydrocarbon receptor (AhR) repressor (AhRR) inhibits the AhR activity. AhRR acts by competing with AhR for heterodimer formation with the AhR nuclear translocator (Arnt) and preventing the AhR·Arnt complex from binding the xenobiotic-responsive elements. Here, we report that AhRR has three evolutionarily conserved SUMOylation consensus sequences within its C-terminal repression domain and that Lys-542, Lys-583, and Lys-660 at the SUMOylation sites are modified by SUMO-1 in vivo. Arginine mutation of the three lysines results in a significant reduction of transcriptional repression activity. SUMOylation of the three lysine residues is important for the interaction between AhRR and ANKRA2, HDAC4, and HDAC5, which are important corepressors for AhRR. Arnt, a heterodimer partner for AhRR, markedly enhanced the SUMOylation of AhRR. AhRR, but not AhR, also significantly enhanced the SUMOylation of Arnt. The SUMOylation of both AhRR and Arnt is important for the efficient transcriptional repression activity of the AhRR/Arnt heterodimer.

Original languageEnglish
Pages (from-to)11017-11026
Number of pages10
JournalJournal of Biological Chemistry
Volume284
Issue number17
DOIs
Publication statusPublished - 2009 Apr 24

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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