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Article

Identification of Ser-386 of interferon regulatory factor 3 as critical target for inducible phosphorylation that determines activation.

The Journal of biological chemistry - 12 Mar 2004

Mori Mitsuaki, Yoneyama Mitsutoshi, Ito Takashi, Takahashi Kiyohiro, Inagaki Fuyuhiko, Fujita Takashi

Abstract excerpt

Interferon regulatory factor (IRF)-3 is a critical transcription factor regulating innate immune responses against viral and bacterial infections. Signals activated by various pathogens are integrated by IRF-3 kinase, resulting in the specific phosphorylation of IRF-3 in the cytoplasm. This phosphorylation induces dimerization and association with the coactivators CREB-binding protein/p300, and the resultant...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 14703513
DOI: 10.1074/jbc.M310616200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Identification of Ser-386 of interferon regulatory factor 3 as critical target for inducible phosphorylation that determines activation.PMID 14703513Read ↗

Interferon regulatory factor 3 is regulated by a dual phosphorylation-dependent switch.Semantic proximity Read ↗

Contribution of Ser386 and Ser396 to activation of interferon regulatory factor 3.Semantic proximity Read ↗

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Identification of the minimal phosphoacceptor site required for in vivo activation of interferon regulatory factor 3 in response to virus and double-stranded RNA.Semantic proximity Read ↗

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Caspase-8-mediated cleavage inhibits IRF-3 protein by facilitating its proteasome-mediated degradation.Semantic proximity Read ↗

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Direct involvement of CREB-binding protein/p300 in sequence-specific DNA binding of virus-activated interferon regulatory factor-3 holocomplex.Semantic proximity Read ↗

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