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 | |
| Publication status | Published - Nov 21 2005 |
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All Science Journal Classification (ASJC) codes
- Immunology and Allergy
- Immunology
Cite this
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
}
TY - JOUR
T1 - PKCβ regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1
AU - Shinohara, Hisaaki
AU - Yasuda, Tomoharu
AU - Aiba, Yuichi
AU - Sanjo, Hideki
AU - Hamadate, Megumi
AU - Watarai, Hiroshi
AU - Sakurai, Hiroaki
AU - Kurosaki, Tomohiro
PY - 2005/11/21
Y1 - 2005/11/21
N2 - 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
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=27944503997&partnerID=8YFLogxK
U2 - 10.1084/jem.20051591
DO - 10.1084/jem.20051591
M3 - Article
C2 - 16301747
AN - SCOPUS:27944503997
VL - 202
SP - 1423
EP - 1431
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
SN - 0022-1007
IS - 10
ER -