The A20-binding protein ABIN-2 exerts unexpected function in mediating transcriptional coactivation

Chia Yi Chien, Wei Kuang Liu, Chen Kung Chou, Jin Yuan Su*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

8 Scopus citations


The human ABIN-2 was originally identified as an A20-associating cytosolic protein to block NF-κB activation induced by various stimuli. Here we report that ABIN-2 has the potential to enter the nucleus and plays a role in mediating transcriptional activation in both yeast and mammalian cells. The Gal4BD-ABIN-2 fusion protein is able to drive the expression of the GAL4-responsive reporter gene in yeast efficiently without the need of the Gal4p activation domain, suggesting that ABIN-2 functions as a transcriptional coactivator and facilitates transcription in yeast. In contrast to the activity in yeast, however, only the C-terminal fragment of ABIN-2 exerts the transactivating activity in mammalian cells but not the full-length ABIN-2 protein. This observation has led to the identification of the N-terminal 195 amino acids of ABIN-2 as a regulatory domain, which retains the full-length ABIN-2 in the cytoplasm of mammalian cells and thus cannot transactivate. We have also found that BAF60a, a component of chromatin-remodeling complex, interacts with ABIN-2 by the yeast two-hybrid analysis. Together, our results suggest that the nuclear ABIN-2 defines a novel transcriptional coactivator and acts presumably by recruiting a chromatin-remodeling complex to the site of the target gene.

Original languageEnglish
Pages (from-to)55-60
Number of pages6
JournalFEBS Letters
Issue number1-3
StatePublished - 22 05 2003
Externally publishedYes


  • ABIN-2
  • BAF60a
  • Chromatin-remodeling complex
  • FLIP1
  • Transcriptional coactivator
  • Yeast two-hybrid


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