NDLI: Par14 protein associates with insulin receptor substrate 1 (IRS-1), thereby enhancing insulin-induced IRS-1 phosphorylation and metabolic actions.

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Par14 protein associates with insulin receptor substrate 1 (IRS-1), thereby enhancing insulin-induced IRS-1 phosphorylation and metabolic actions.

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Par14 protein associates with insulin receptor substrate 1 (IRS-1), thereby enhancing insulin-induced IRS-1 phosphorylation and metabolic actions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Takahashi, Shin-ichiro Otani, Yuichiro Nakatsu, Yusuke Guo, Ying Sakoda, Hideyuki Fukushima, Toshiaki Yamamotoya, Takeshi Tsuchiya, Yoshihiro Asano, Tomoichiro Iwashita, Misaki Kushiyama, Akifumi Fujishiro, Midori Katagiri, Hideki Kamata, Hideaki Shinjo, Takanori Kurihara, Hiroki Uchida, Takafumi Okubo, Hirofumi Nishimura, Fusanori Zhang, Jun
Description	Author Affiliation: Zhang J ( Department of Medical Science, Graduate School of Medicine, University of Hiroshima, 1-2-3 Kasumi, Minami-ku, 734-8553 Hiroshima City, 734-8553 Hiroshima, Japan.)
Abstract	Pin1 and Par14 are parvulin-type peptidyl-prolyl cis/trans isomerases. Although numerous proteins have been identified as Pin1 substrates, the target proteins of Par14 remain largely unknown. Par14 expression levels are increased in the livers and embryonic fibroblasts of Pin1 KO mice, suggesting a compensatory relationship between the functions of Pin1 and Par14. In this study, the association of Par14 with insulin receptor substrate 1 (IRS-1) was demonstrated in HepG2 cells overexpressing both as well as endogenously in the mouse liver. The analysis using deletion-mutated Par14 and IRS-1 constructs revealed the N-terminal portion containing the basic domain of Par14 and the two relatively C-terminal portions of IRS-1 to be involved in these associations, in contrast to the WW domain of Pin1 and the SAIN domain of IRS-1. Par14 overexpression in HepG2 markedly enhanced insulin-induced IRS-1 phosphorylation and its downstream events, PI3K binding with IRS-1 and Akt phosphorylation. In contrast, treating HepG2 cells with Par14 siRNA suppressed these events. In addition, overexpression of Par14 in the insulin-resistant ob/ob mouse liver by adenoviral transfer significantly improved hyperglycemia with normalization of hepatic PEPCK and G6Pase mRNA levels, and gene suppression of Par14 using shRNA adenovirus significantly exacerbated the glucose intolerance in Pin1 KO mice. Therefore, although Pin1 and Par14 associate with different portions of IRS-1, the prolyl cis/trans isomerization in multiple sites of IRS-1 by these isomerases appears to be critical for efficient insulin receptor-induced IRS-1 phosphorylation. This process is likely to be one of the major mechanisms regulating insulin sensitivity and also constitutes a potential therapeutic target for novel insulin-sensitizing agents.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	28
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-07-12
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Insulin Receptor Substrate Proteins Metabolism Insulin Pharmacology Peptidylprolyl Isomerase Animals Binding Sites Genetics Glucose Intolerance HEK293 Cells Hep G2 Cells Hyperglycemia Therapy Hypoglycemic Agents Immunoblotting Liver Mice Mice, Inbred C57BL Mice, Knockout Mice, Obese Mutation Obesity Blood Phosphatidylinositol 3-Kinases Phosphorylation Drug Effects Protein Binding Proto-Oncogene Proteins C-akt RNA Interference Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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