PKCβ regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1
Copyright policy )PKCβ regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1
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.
Molecular Sequence Data, Receptors, Antigen, B-Cell, MAP Kinase Kinase Kinases, Article, Cell Line, I-kappa B Kinase, CARD Signaling Adaptor Proteins, Mice, Guanylate Cyclase, Protein Kinase C beta, Animals, Amino Acid Sequence, Phosphorylation, Apoptosis Regulatory Proteins, Chickens, Protein Kinase C
Molecular Sequence Data, Receptors, Antigen, B-Cell, MAP Kinase Kinase Kinases, Article, Cell Line, I-kappa B Kinase, CARD Signaling Adaptor Proteins, Mice, Guanylate Cyclase, Protein Kinase C beta, Animals, Amino Acid Sequence, Phosphorylation, Apoptosis Regulatory Proteins, Chickens, Protein Kinase C
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