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J. Biochem, 2003, Vol. 133, No. 2 181-187
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Regulation of a Mitogen-Activated Protein Kinase Kinase Kinase, MLTK by PKN

Mikiko Takahashi1, Yusuke Gotoh2, Takayuki Isagawa2, Tamako Nishimura2, Emiko Goyama2, Hon-Song Kim2, Hideyuki Mukai1,2 and Yoshitaka Ono+,1,2

1 Biosignal Research Center and 2 Graduate School of Science and Technology, Kobe University, Kobe 657-8501

PKN{alpha} is a fatty acid- and Rho-activated serine/threonine protein kinase having a catalytic domain homologous to members of the protein kinase C family. Recently it was reported that PKN{alpha} is involved in the p38 mitogen–activated protein kinase (MAPK) signaling pathway. To date, however, how PKN{alpha} regulates the p38{gamma} MAPK signaling pathway is unclear. Here we demonstrate that PKN{alpha} efficiently phosphorylates MLTK{alpha} (MLK-like mitogen-activated protein triple kinase), which was recently identified as a MAPK kinase kinase (MAPKKK) for the p38 MAPK cascade. Phosphorylation of MLTK{alpha} by PKN{alpha} enhances its kinase activity in vitro. Expression of the kinase-negative mutant of PKN{alpha} inhibited the mobility shift of MLTK{alpha} caused by osmotic shock in SDS-PAGE. Furthermore, PKN{alpha} associates with each member of the p38{gamma} MAPK signaling pathway (p38{gamma}, MKK6, and MLTK{alpha}). These results suggest that PKN{alpha} functions as not only an upstream activator of MLTK{alpha} but also a putative scaffold protein for the p38{gamma} MAPK signaling pathway.

+ To whom correspondence should be addressed. Tel: +81-78-803-5792, Fax: +81-78-803-5782, E-mail: yonodayo{at}kobe-u.ac.jp


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