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

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

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

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

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 complex activates the target genes in the nucleus. However, the phosphorylation sites that determine the active/inactive status of IRF-3 have been a source of controversy. In this study, we generated an antibody that specifically detects the phosphorylation of Ser-386 and used it as a probe. We found: 1) viral infection specifically induces phosphorylation of the Ser-386; 2) recently identified IRF-3 kinases (IKK-i/epsilon and TBK-1) phosphorylate Ser-386 and induce its dimerization; 3) phosphorylation of Ser-386 is exclusively observed with the dimer; 4) mutation at Ser-386 abolishes the dimerization potential; 5) a constitutively active 5D mutant designed to mimic phosphorylation of Ser/Thr residues other than Ser-385 and -386 is secondarily phosphorylated at Ser-386, presumably by an irrelevant kinase. These results strongly suggest that Ser-386 is the target of the IRF-3 kinase and critical determinant for the activation of IRF-3.

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

M Mori,M Yoneyama,T Ito,K Takahashi,F Inagaki,T Fujita,

For similar investigative techniques: genetic techniques: gene transfer techniques: transfection research abstracts see: investigative techniques: genetic techniques: gene transfer techniques: transfection research

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

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 279

Page Numbers: 9698-702

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 31

MONTH: 12

YEAR: 2003

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

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

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

KEYWORDS: Transfection

MESH TERMS: chemistry

Chemical & Substance for Abstract: Identification of Ser-386 of interferon regulatory factor 3 as critical target for inducible phosphorylation that determines activation. Information

Substance Name: TBK1 protein, human

Registry Number: EC 2.7.11.1

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

AFFILIATION: Department of Tumor Cell Biology, The Tokyo Metropolitan Institute of Medical Science, Japan.

Country: United States

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MEDLINETA: J Biol Chem

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