WIP1 phosphatase is a critical regulator of adipogenesis through dephosphorylating PPAR γ serine 112.

WIP1 phosphatase is a critical regulator of adipogenesis through dephosphorylating PPARγ serine 112. Cell Mol Life Sci. 2017 Feb 08;: Authors: Li D, Zhang L, Xu L, Liu L, He Y, Zhang Y, Huang X, Zhao T, Wu L, Zhao Y, Wu K, Li H, Yu X, Zhao T, Gong S, Fan M, Zhu L Abstract WIP1, as a critical phosphatase, plays many important roles in various physiological and pathological processes through dephosphorylating different substrate proteins. However, the functions of WIP1 in adipogenesis and fat accumulation are not clear. Here, we report that WIP1-deficient mice show impaired body weight growth, dramatically decreased fat mass, and significantly reduced triglyceride and leptin levels in circulation. This dysregulation of adipose development caused by the deletion of WIP1 occurs as early as adipogenesis. In contrast, lentivirus-mediated WIP1 phosphatase overexpression significantly increases the adipogenesis of pre-adipocytes via an enzymatic activity-dependent mechanism. PPARγ is a master gene of adipogenesis, and the phosphorylation of PPARγ at serine 112 strongly inhibits adipogenesis; however, very little is known about the negative regulation of this phosphorylation. Here, we show that WIP1 phosphatase plays a pro-adipogenic role by interacting directly with PPARγ and dephosphorylating p-PPARγ S112 in vitro and in vivo. PMID: 28180926 [PubMed - as supplied by publisher]
Source: Cellular and Molecular Life Sciences : CMLS - Category: Cytology Authors: Tags: Cell Mol Life Sci Source Type: research
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