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Nucleic Acids Research 2005 33(11):3561-3569; doi:10.1093/nar/gki667
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Published online 24 June 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

EID3 is a novel EID family member and an inhibitor of CBP-dependent co-activation

Ann Båvner*, Jason Matthews, Sabyasachi Sanyal, Jan-Åke Gustafsson and Eckardt Treuter

Department of Biosciences at Novum, Karolinska Institutet S-14157 Huddinge, Sweden

*To whom correspondence should be addressed. Tel: +46 8 6089160; Fax: +46 8 7745538; Email: ann.bavner{at}biosci.ki.se

Revised June 2, 2005. Accepted June 6, 2005.

EID1 (E1A-like inhibitor of differentiation 1) functions as an inhibitor of nuclear receptor-dependent gene transcription by directly binding to co-regulators. Alternative targets include the co-repressor small heterodimer partner (SHP, NR0B2) and the co-activators CBP/p300, indicating that EID1 utilizes different inhibitory strategies. Recently, EID2 was characterized as an inhibitor of muscle differentiation and as an antagonist of both CBP/p300 and HDACs. Here, we describe a third family member designated EID3 that is highly expressed in testis and shows homology to a region of EID1 implicated in binding to CBP/p300. We demonstrate that EID3 acts as a potent inhibitor of nuclear receptor transcriptional activity by a mechanism that is independent of direct interactions with nuclear receptors, including SHP. Furthermore, EID3 directly binds to and blocks the SRC-1 interacting domain of CBP, which has been implicated to act as the interaction surface for nuclear receptor co-activators. Consistent with this idea, EID3 prevents recruitment of CBP to a natural nuclear receptor-regulated promoter. Our study suggests that EID-family members EID3 and EID1 act as inhibitors of CBP/p300-dependent transcription in a tissue-specific manner.

DDBJ/EMBL/GenBank accession nos AAH27612 and NM_025499


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