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J. Biol. Chem., Vol. 277, Issue 35, 31871-31876, August 30, 2002

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Protein Kinase C-associated Kinase (PKK) Mediates Bcl10-independent NF-B Activation Induced by Phorbol Ester^*

Akihiro Muto^§, Jürgen Ruland^¶, Linda M. McAllister-Lucas^**, Peter C. Lucas, Shoji Yamaoka^§§, Felicia F. Chen, Amy Lin^¶, Tak W. Mak^¶, Gabriel Núñez^¶¶, and Naohiro Inohara^¶¶

From the  Department of Pathology and Comprehensive Cancer Center,  Department of Pediatrics and Communicable Diseases, University of Michigan Medical School, Ann Arbor, Michigan 48109, the ^¶ Amgen Institute and Ontario Cancer Institute and Departments of Medical Biophysics and Immunology, University of Toronto, Ontario M5G 2C1, Canada, and the ^§§ Department of Microbiology, Tokyo Medical and Dental University, School of Medicine, Yushima 1-5-45, Bunkyo-ku, Tokyo 113-8519, Japan

Protein kinase C-associated kinase (PKK) is a recently described kinase of unknown function that was identified on the basis of its specific interaction with PKC. PKK contains N-terminal kinase and C-terminal ankyrin repeats domains linked to an intermediate region. Here we report that the kinase domain of PKK is highly homologous to that of two mediators of nuclear factor-B (NF-B) activation, RICK and RIP, but these related kinases have different C-terminal domains for binding to upstream factors. We find that expression of PKK, like RICK and RIP, induces NF-B activation. Mutational analysis revealed that the kinase domain of PKK is essential for NF-B activation, whereas replacement of serine residues in the putative activation loop did not affect the ability of PKK to activate NF-B. A catalytic inactive PKK mutant inhibited NF-B activation induced by phorbol ester and Ca²⁺-ionophore, but it did not block that mediated by tumor necrosis factor , interleukin-1, or Nod1. Inhibition of NF-B activation by dominant negative PKK was reverted by co-expression of PKCI, suggesting a functional association between PKK and PKCI. PKK-mediated NF-B activation required IKK and IKK but not IKK, the regulatory subunit of the IKK complex. Moreover, NF-B activation induced by PKK was not inhibited by dominant negative Bimp1 and proceeded in the absence of Bcl10, two components of a recently described PKC signaling pathway. These results suggest that PKK is a member of the RICK/RIP family of kinases, which is involved in a PKC-activated NF-B signaling pathway that is independent of Bcl10 and IKK.

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