We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
The A20-binding protein ABIN-2 exerts unexpected function in mediating transcriptional coactivation
- Authors
Chien, Chia-Yi; Liu, Wei-Kuang; Chou, Chen-Kung; Su, Jin-Yuan
- Abstract
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.
- Subjects
PROTEINS; YEAST
- Publication
FEBS Letters, 2003, Vol 543, Issue 1-3, p55
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(03)00401-0