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IRF2-binding protein-1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2-dependent transcription

Authors :
Makoto Kimura
Source :
FEBS letters. 582(19)
Publication Year :
2008

Abstract

Jun-dimerization protein 2 (JDP2) is a member of the activating protein-1 (AP-1) family of transcription factors. JDP2 dimerizes with other AP-1 proteins such as activating transcription factor-2 (ATF2) and Jun to repress transcription from promoters that contain a cyclic AMP-responsive element (CRE). Interferon regulatory factor-2-binding protein-1 (IRF2-BP1), which is reported to be a transcriptional corepressor of IRF2, was isolated as a JDP2-binding protein using an epitope-tagging method. As anticipated from the presence of a RING-finger domain, IRF2-BP1 enhanced the polyubiquitination of JDP2. Moreover, IRF2-BP1 repressed ATF2-mediated transcriptional activation from a CRE-containing promoter.Structured summaryMINT-6699624:JDP2 (uniprotkb:Q8WYK2) physically interacts (MI:0218) with Valyl-tRNA synthetase (uniprotkb:P26640), IRF2-BP1 (uniprotkb:Q8IU81), ATF7 (uniprotkb:P17544), EEF1G (uniprotkb:P26641), EEF1A1 (uniprotkb:P68104), JUND (uniprotkb:P17535), JUNB (uniprotkb:P17275), EF1D2 (uniprotkb:P29692) and RPLP0 (uniprotkb:P05388) by anti tag coimmunoprecipitation (MI:0007).MINT-6699850:JDP2 (uniprotkb:Q8WYK2) binds (MI:0407) to IRF2-BP1 (uniprotkb:Q8IU81) by pull down (MI:0096).MINT-6699684:JDP2 (uniprotkb:Q8WYK2) physically interacts (MI:0218) with JUNB (uniprotkb:P17275), JUND (uniprotkb:P17535), ATF7 (uniprotkb:P17544) and IRF2-BP1 (uniprotkb:Q8IU81) by anti tag coimmunoprecipitation (MI:0007).MINT-6699839:IRF2-BP1 (uniprotkb:Q8IU81) physically interacts (MI:0218) with JDP2 (uniprotkb:Q8WYK2) by anti bait coimmunoprecipitation (MI:0006).MINT-6699748:JDP2 (uniprotkb:Q8WYK2) physically interacts (MI:0218) with ATF2 (uniprotkb:P15336) and c-JUN (uniprotkb:P05412) by anti tag coimmunoprecipitation (MI:0007).MINT-6699865:ATF2 (uniprotkb:P15336) binds (MI:0407) to IRF2-BP1 (uniprotkb:Q8IU81) by pull down (MI:0096).

Details

ISSN :
00145793
Volume :
582
Issue :
19
Database :
OpenAIRE
Journal :
FEBS letters
Accession number :
edsair.doi.dedup.....be00761ba146fcd08e1ac781033dbf5c