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Originally published In Press as doi:10.1074/jbc.M211770200 on March 6, 2003

J. Biol. Chem., Vol. 278, Issue 20, 18440-18447, May 16, 2003
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Adipose-specific Expression, Phosphorylation of Ser794 in Insulin Receptor Substrate-1, and Activation in Diabetic Animals of Salt-inducible Kinase-2*

Nanao Horikeabc, Hiroshi Takemoriab, Yoshiko Katohac, Junko Doiad, Li Mina, Tomoichiro Asanoe, Xiao Jian Sunf, Hiroyasu Yamamotog, Soji Kasayamag, Masaaki Muraokaah, Yasuki Nonakai, and Mitsuhiro Okamotoajk

From the a Department of Biochemistry and Molecular Biology (H-1) and g Department of Molecular Medicine (C-4), Graduate School of Medicine, and j Laboratories for Biomolecular Networks, Graduate School of Frontier Biosciences, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan, the d Department of Life Science, Kinran College, Suita, Osaka 565-0873, Japan, the e Department of Internal Medicine, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan, and f Endocrinology Division, College of Medicine, University of Vermont, Burlington, Vermont 05405, h ProteinExpress Co., Ltd., 2-11 Chuo-cho, Choshi, Chiba 288-0041, Japan, and i College of Nutrition, Koshien University, Takarazuka, Hyogo, 665-0006, Japan

Salt-inducible kinase (SIK), first cloned from the adrenal glands of rats fed a high salt diet, is a serine/threonine protein kinase belonging to an AMP-activated protein kinase family. Induced in Y1 cells at an early stage of ACTH stimulation, it regulated the initial steps of steroidogenesis. Here we report the identification of its isoform SIK2. When a green fluorescent protein-fused SIK2 was expressed in 3T3-L1 preadipocytes, it was mostly present in the cytoplasm. When coexpressed in cAMP-responsive element-reporter assay systems, SIK2 could repress the cAMP-responsive element-dependent transcription, although the degree of repression seemed weaker than that by SIK1. SIK2 was specifically expressed in adipose tissues. When 3T3-L1 cells were treated with the adipose differentiation mixture, SIK2 mRNA was induced within 1 h, the time of induction almost coinciding with that of c/EBPbeta mRNA. Coexpressed with human insulin receptor substrate-1 (IRS-1) in COS cells, SIK2 could phosphorylate Ser794 of human IRS-1. Adenovirus-mediated overexpression of SIK2 in adipocytes elevated the level of phosphorylation at Ser789, the mouse equivalent of human Ser794. Moreover, the activity and content of SIK2 were elevated in white adipose tissues of db/db diabetic mice. These results suggest that highly expressed SIK2 in insulin-stimulated adipocytes phosphorylates Ser794 of IRS-1 and, as a result, might modulate the efficiency of insulin signal transduction, eventually causing the insulin resistance in diabetic animals.

* This work was supported in part by grants-in-aid for Scientific Research from the Ministry of Education, Culture, Sports, Science, and Technology, the Ministry of Health, Labor, and Welfare Japan, grants from The Uehara Memorial Foundation, The Salt Science Research Foundation Grant 0238, grants from CREST Project of JPST for "Endocrine Disruption on Action of Brain Neurosteroids," and by "21st Century Center of Excellence" grant of Japan (to L. M.).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.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AB067780.

b Both authors contributed equally to this work.

c Research fellows of the Japan Society for the Promotion of Science.

k To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Graduate School of Medicine (H-1), Osaka University, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan. Tel.: 81-6-6879-3280; Fax: 81-6-6879-3289; E-mail: mokamoto@mr-mbio.med.osaka-u.ac.jp.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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