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Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo.

The members of the AP-2 family of transcription factors are developmentally regulated and have distinct yet overlapping functions in the regulation of many genes governing growth and differentiation. All AP-2 factors appear to be capable of binding very similar DNA recognition sites, and the determinants of functional specificity remain to be elucidated. AP-2 transcription factors have been shown to act both as transcriptional activators and repressors in a promoter-specific manner. Although several mediators of their activation function have been suggested, few mechanisms for the repression or down-regulation of transactivation have been described. In a two-hybrid screen for proteins interacting with AP-2 factors, we have identified the UBC9 gene that encodes the E2 (ubiquitin carrier protein)-conjugating enzyme for the small ubiquitin-like modifier, SUMO. The interaction domain resides in the C-terminal half of AP-2, which contains the conserved DNA binding and dimerization domains. We have detected sumolated forms of endogenous AP-2 in mammalian cells and have further mapped the in vivo sumolation site to conserved lysine 10. Transient transfection studies indicate that sumolation of AP-2 decreases its transcription activation potential, and we discuss the possible mechanisms for the observed suppression of AP-2 transactivation.

Pubmed ID: 12072434

Authors

  • Eloranta JJ
  • Hurst HC

Journal

The Journal of biological chemistry

Publication Data

August 23, 2002

Associated Grants

None

Mesh Terms

  • Cell Line
  • DNA-Binding Proteins
  • Humans
  • Ligases
  • Lysine
  • SUMO-1 Protein
  • Transcription Factor AP-2
  • Transcription Factors
  • Transcription, Genetic
  • Ubiquitin-Conjugating Enzymes