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Ikaros Interactions with CtBP Reveal a Repression Mechanism That Is Independent of Histone Deacetylase Activity

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Koipally, Joseph, Georgopoulos, Katia·2000·Journal of Biological Chemistry

Abstract

We have previously shown that Ikaros can repress transcription through the recruitment of histone deacetylase complexes. Here we provide evidence that Ikaros can also repress transcription through its interactions with the co-repressor, C-terminal binding protein (CtBP). CtBP interacts with Ikaros isoforms through a PEDLS motif present at the N terminus of these proteins but not with homologues like Aiolos which lack this motif. Mutations in Ikaros that prevent CtBP interactions reduce its ability to repress transcription. CtBP interacts with Sin3A but not with the Mi-2 co-repressor and it represses transcription in a manner that is independent of histone deacetylase activity. These data strongly suggest that CtBP contributes to a histone deacetylase activity independent mechanism of repression by Ikaros. Finally, we show that the viral oncoprotein E1A, which binds to CtBP, also shows a strong association with Ikaros. This Ikaros-E1A interaction may underlie Ikaros's decreased ability to repress transcription in E1A transformed cells.

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Metadata

Authors
Koipally, J., & Georgopoulos, K.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2000-06
Volume
275
Issue
26
Pages
19594-19602
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2018170238
Cited by
193
References
4
FWCI
6.98
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Ikaros Interactions with CtBP Reveal a Repression Mechanism That Is Independent of Histone Deacetylase Activity. https://app.cochat.ai/papers/10.1074/jbc.m000254200
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Koipally, J., & Georgopoulos, K. (2000). Ikaros Interactions with CtBP Reveal a Repression Mechanism That Is Independent of Histone Deacetylase Activity. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m000254200

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