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

Research output: Contribution to journalArticlepeer-review

130 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 languageEnglish
Pages (from-to)1423-1431
Number of pages9
JournalJournal of Experimental Medicine
Volume202
Issue number10
DOIs
Publication statusPublished - Nov 21 2005
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology

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