PKCβ regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1

Hisaaki Shinohara; Tomoharu Yasuda; Yuichi Aiba; Hideki Sanjo; Megumi Hamadate; Hiroshi Watarai; Hiroaki Sakurai; Tomohiro Kurosaki

doi:10.1084/jem.20051591

PKCβ regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1

Hisaaki Shinohara, Tomoharu Yasuda, Yuichi Aiba, Hideki Sanjo, Megumi Hamadate, Hiroshi Watarai, Hiroaki Sakurai, Tomohiro Kurosaki

Department of Molecular and Structural Biology

Research output: Contribution to journal › Article › peer-review

126 Citations (Scopus)

Abstract

The B cell antigen receptor (BCR)-mediated activation of IΚB kinase (IKK) and nuclear factor-ΚB require protein kinase C (PKC)β; however, the mechanism by which PKCβ regulates IKK is unclear. Here, we demonstrate that another protein kinase, TGFβ-activated kinase (TAK)1, is essential for IKK activation in response to BCR stimulation. TAK1 interacts with the phosphorylated CARMA1 (also known as caspase recruitment domain [CARD]11, Bimp3) and this interaction is mediated by PKCβ. IKK is also recruited to the CARMA1-Bcl10-mucosal-associated lymphoid tissue 1 adaptor complex in a PKCβ-dependent manner. Hence, our data suggest that phosphorylation of CARMA1, mediated by PKCβ, brings two key protein kinases, TAK1 and IKK, into close proximity, thereby allowing TAK1 to phosphorylate IKK. JEM

Original language	English
Pages (from-to)	1423-1431
Number of pages	9
Journal	Journal of Experimental Medicine
Volume	202
Issue number	10
DOIs	https://doi.org/10.1084/jem.20051591
Publication status	Published - Nov 21 2005

All Science Journal Classification (ASJC) codes

Immunology and Allergy
Immunology

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10.1084/jem.20051591

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PKCβ regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1. / Shinohara, Hisaaki; Yasuda, Tomoharu; Aiba, Yuichi; Sanjo, Hideki; Hamadate, Megumi; Watarai, Hiroshi; Sakurai, Hiroaki; Kurosaki, Tomohiro.

In: Journal of Experimental Medicine, Vol. 202, No. 10, 21.11.2005, p. 1423-1431.

Research output: Contribution to journal › Article › peer-review

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title = "PKCβ regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1",

abstract = "The B cell antigen receptor (BCR)-mediated activation of IΚB kinase (IKK) and nuclear factor-ΚB require protein kinase C (PKC)β; however, the mechanism by which PKCβ regulates IKK is unclear. Here, we demonstrate that another protein kinase, TGFβ-activated kinase (TAK)1, is essential for IKK activation in response to BCR stimulation. TAK1 interacts with the phosphorylated CARMA1 (also known as caspase recruitment domain [CARD]11, Bimp3) and this interaction is mediated by PKCβ. IKK is also recruited to the CARMA1-Bcl10-mucosal-associated lymphoid tissue 1 adaptor complex in a PKCβ-dependent manner. Hence, our data suggest that phosphorylation of CARMA1, mediated by PKCβ, brings two key protein kinases, TAK1 and IKK, into close proximity, thereby allowing TAK1 to phosphorylate IKK. JEM",

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AU - Shinohara, Hisaaki

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AU - Aiba, Yuichi

AU - Sanjo, Hideki

AU - Hamadate, Megumi

AU - Watarai, Hiroshi

AU - Sakurai, Hiroaki

AU - Kurosaki, Tomohiro

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