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I{kappa}B kinase induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells.

I{kappa}B kinase induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells. Research Abstract Details 

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  • I{kappa}B kinase induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells. Abstract Text:

    hisaaki shinoharaHisaaki Shinohara,shiori maedaShiori Maeda,hiroshi wataraiHiroshi Watarai,tomohiro kurosakiTomohiro Kurosaki,hisaaki shinoharaHisaaki Shinohara,shiori maedaShiori Maeda,hiroshi wataraiHiroshi Watarai,tomohiro kurosakiTomohiro Kurosaki,hisaaki shinoharaHisaaki Shinohara,shiori maedaShiori Maeda,hiroshi wataraiHiroshi Watarai,tomohiro kurosakiTomohiro Kurosaki,

    Protein kinase C (PKC) beta has been reported (Shinohara, H., T. Yasuda, Y. Aiba, H. Sanjo, M. Hamadate, H. Watarai, H. Sakurai, and T. Kurosaki. 2005. J. Exp. Med. 202:1423-1431; Sommer, K., B. Guo, J.L. Pomerantz, A.D. Bandaranayake, M.E. Moreno-Garcia, Y.L. Ovechkina, and D.J. Rawlings. 2005. Immunity. 23:561-574) to play a crucial role in B cell receptor (BCR)-mediated IkappaB kinase (IKK) activation through phosphorylation of caspase recruitment domain 11, Bimp3 (CARMA1). However, it remains unclear whether this PKCbeta-mediated phosphorylation accounts fully for the activation status of CARMA1, because involvement of other kinases, such as phosphoinositide 3-kinase-dependent kinase 1, has also been suggested. We show that PKCbeta mediates phosphorylation of CARMA1 on Ser668, which in turn is essential for BCR-mediated CARMA1-Bcl10-mucosal-associated lymphoid tissue 1 (MALT1) association and subsequent IKK activation. Our analyses also demonstrate that the downstream kinase IKKbeta contributes to facilitating formation of the complex CARMA1-Bcl10-MALT1 by mediating phosphorylation of CARMA1. Hence, our data suggest that PKCbeta is crucial for initial activation of IKK. The activated IKKbeta does not merely function as an effector enzyme but also modifies the upstream signaling complex through a feedback mechanism, thereby optimizing the strength and duration of the nuclear factor kappaB signal.

    I{kappa}B kinase induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells. Publishing Authors By Initials

    h shinoharaH Shinohara,s maedaS Maeda,h wataraiH Watarai,t kurosakiT Kurosaki,h shinoharaH Shinohara,s maedaS Maeda,h wataraiH Watarai,t kurosakiT Kurosaki,h shinoharaH Shinohara,s maedaS Maeda,h wataraiH Watarai,t kurosakiT Kurosaki,

    For similar abstracts research abstracts see: abstracts research

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    I{kappa}B kinase induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: The Journal of experimental medicine

    VOLUME: 204

    Page Numbers: 3285-93

    Journal Abbreviation: J. Exp. Med.

    ISSN: 1540-9538

    DAY: 17

    MONTH: 12

    YEAR: 2007

    I{kappa}B kinase induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells. Information

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    LANGUAGE: eng

    NlmUniqueID: 2985109

    I{kappa}B kinase induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells. Keywords Mesh Terms:

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    Grant and Affiliation Information for I{kappa}B kinase induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells.

    AFFILIATION: Laboratory for Lymphocyte Differentiation and 2Laboratory for Immune Regulation, RIKEN Research Center for Allergy and Immunology, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Exp Med

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