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J. Biol. Chem., Vol. 278, Issue 14, 12013-12021, April 4, 2003
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From the Although TAK1 signaling plays essential roles in
eliciting cellular responses to interleukin-1 (IL-1), a proinflammatory
cytokine, how the IL-1-TAK1 signaling pathway is positively and
negatively regulated remains poorly understood. In this study, we
investigated the possible role of a novel protein phosphatase 2C (PP2C)
family member, PP2C The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY184801.
Regulation of the Interleukin-1-induced Signaling Pathways by a
Novel Member of the Protein Phosphatase 2C Family (PP2C
)*
,,
,, and§§
Department of Biochemistry, Institute of
Development, Aging, and Cancer, Tohoku University, 4-1 Seiryomachi,
Aoba-ku, Sendai 980-8575, Japan, the § Biological Resources
Division, Japan International Research Center for Agricultural
Sciences, 1-1 Ohwashi, Tsukuba 305-0851, Japan, the ¶ Department
of Biochemistry, Kumamoto University Medical School, Honjo, Kumamoto
860-0811, Japan, the Department of Environmental and Molecular
Toxicology, North Carolina State University, Raleigh, North
Carolina 27695-7633, and the ** Department of Molecular
Biology, Graduate School of Science, Nagoya University, Chikusa-ku,
Nagoya 464-8602, Japan
, in the regulation of the IL-1-TAK1 signaling
pathway. PP2C was composed of 303 amino acids, and the overall
similarity of amino acid sequence between PP2C and PP2C
was found
to be 26%. Ectopic expression of PP2C inhibited the IL-1- and
TAK1-induced activation of mitogen-activated protein kinase kinase 4 (MKK4)-c-Jun N-terminal kinase or MKK3-p38 signaling pathway. PP2C
dephosphorylated TAK1 in vitro. Co-immunoprecipitation
experiments indicated that PP2C associates stably with TAK1 and
attenuates the binding of TAK1 to MKK4 or MKK6. Ectopic expression of a
phosphatase-negative mutant of PP2C, PP2C(D/A), which acted as a
dominant negative form, enhanced both the association between TAK1 and
MKK4 or MKK6 and the TAK1-induced activation of an AP-1 reporter gene.
The association between PP2C and TAK1 was transiently suppressed by
IL-1 treatment of the cells. Taken together, these results suggest
that, in the absence of IL-1-induced signal, PP2C contributes to
keeping the TAK1 signaling pathway in an inactive state by associating
with and dephosphorylating TAK1.
*
This work was supported in part by a Grant-in-Aid for
Scientific Research from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence may be addressed. Tel.: 81-22-717-8471;
Fax: 81-22-717-8476; E-mail: takayasu@idac.tohoku.ac.jp.
§§
To whom correspondence may be addressed. Tel.: 81-22-717-8471;
Fax: 81-22-717-8476; E-mail:
tamura@idac.tohoku.ac.jp.
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