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CIDE Proteins and Metabolic Disorders Jingyi Gong, Zhiqi Sun and Peng Li

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CIDE Proteins and Metabolic Disorders Jingyi Gong, Zhiqi Sun and Peng Li CIDE proteins and metabolic disorders Jingyi Gong, Zhiqi Sun and Peng Li Protein Science Laboratory of Ministry of Education, Purpose of review Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, China The cell death-inducing DFF45-like effector (CIDE) family proteins, comprising three members, Cidea, Cideb, and Fsp27 (Cidec), have emerged as important regulators for Correspondence to Dr Peng Li, Department of Biological Sciences and Biotechnology, Tsinghua various aspects of metabolism. This review summarizes our current understanding University, Beijing 100084, China about the physiological roles of CIDE proteins, their transcriptional regulations, and their Tel/fax: +86 10 62797121; e-mail: [email protected] underlying mechanism in controlling the development of metabolic disorders. Recent findings Current Opinion in Lipidology 2009, 20:121–126 Animals with deficiency in Cidea, Cideb, and Fsp27 all display lean phenotypes with higher energy expenditure and are resistant to diet-induced obesity and insulin resistance. CIDE proteins, localized to lipid droplets and endoplasmic reticulum, control lipid metabolism in adipocytes and hepatocytes through regulating AMP-activated protein kinase stability and influencing lipogenesis or lipid droplet formation. The expression of CIDE proteins is controlled at both transcriptional and posttranslational levels and positively correlates with the development of obesity, liver steatosis, and insulin sensitivity in both rodents and humans. Summary CIDE proteins are important regulators of energy homeostasis and are closely linked to the development of metabolic disorders including obesity, diabetes, and liver steatosis. They may serve as potential molecular targets for the screening of therapeutic drugs for these diseases. Keywords Cidea, Cideb, Fsp27, lipid droplets, metabolic disorders Curr Opin Lipidol 20:121–126 ß 2009 Wolters Kluwer Health | Lippincott Williams & Wilkins 0957-9672 proteins that are ubiquitously expressed, CIDE family Introduction proteins have distinct tissue expression patterns with Metabolic disorders including obesity, hyperlipidemia, Cidea in BAT in rodents [3], Cideb [4] in liver, and insulin resistance, liver steatosis, and hypertension are a Fsp27 in WAT and BAT [3,5,6]. Cidea mRNA is group of diseases associated with metabolic malfunction detected in human WAT tissues, which might reflect a and unbalanced energy homeostasis. The cell death- heterogeneous nature of human WAT [7]. Interestingly, inducing DFF45-like effector (CIDE) proteins, Cidea, mRNAs of Fsp27 and Cidea were also detected in fatty Cideb and Fsp27, are predominantly expressed in brown livers in which excess amount of lipid is accumulated and adipose tissue (BAT), liver and white adipose tissues large lipid droplets are formed [8–10]. (WATs). Studies using animals deficient in CIDE proteins have demonstrated that this class of proteins plays import- CIDE proteins are subjected to tight regulation on both ant roles in lipid storage, lipid droplet formation, lipolysis transcriptional and posttranslational levels. Fsp27 is and the development of obesity, diabetes, and liver stea- expressed in differentiated white adipocytes [5,11,12] tosis. Here we summarize recent findings on the CIDE and controlled by transcription factors CCAAT/enhancer proteins, with particular emphasis on their molecular binding protein (C/EBP) and peroxisome proliferator- mechanisms in controlling energy homeostasis. activated receptor (PPARg) [8,11]. TNF-a, a negative regulator of C/EBP, reduced the Fsp27 gene expression [13]. Cidec, a human homolog of rodent Fsp27, is induced Tissue distribution and transcriptional by PPARg2 [14]. Retinoid X receptor (RXR) also binds to regulation of CIDE proteins the Fsp27 promoter region in a PPARgg-dependent CIDE proteins contain an evolutionary conserved CIDE- manner [15]. In liver, Fsp27 is a direct target of PPARg N domain that shares homology to the DNA fragment [9]. Cidea promoter region contains both PPARa and factor 40/45 (DFF40/45) [1] and a CIDE-C domain that is PPARg response elements and can be activated by PPAR unique among CIDE proteins [2]. Unlike DFF40/45 agonist [10]. In addition, PGC-1a can activate Cidea 0957-9672 ß 2009 Wolters Kluwer Health | Lippincott Williams & Wilkins DOI:10.1097/MOL.0b013e328328d0bb 122 Genetics and molecular biology expression through binding to estrogen-related receptor and ectopic expression of Cideb induces caspase-inde- alpha (ERRa) and nuclear respiratory factor-1 (NRF-1), pendent cell death in a dimer-dependent manner [23]. while RIP140, a corepressor of nuclear receptors, inter- Cideb expression was also correlated with neuronal apop- acts with PGC-1a and represses its transcriptional tosis after nerve injury [32]. Furthermore, Cideb was activity on Cidea promoter [16,17]. Investigation in tumor shown to interact with NS2, a nonstructural protein cells indicates that CpG methylation on the Cidea pro- encoded by HCV, which inhibits Cideb-induced cell moter region may play a crucial role in establishing death [33]. Furthermore, Cidea could regulate apoptosis and maintaining tissue-specific and cell-specific Cidea induced by TGF-b pathway in human breast epithelial expression [18]. TNF-a negatively regulates transcrip- cells [22]. In addition, Fsp27 and Cidec were reported to tion of Cidea through NF-kB activation [19]. The play a role in cell death and tumorigenesis [34,35]. expression of human Cideb is regulated by upstream and internal promoters. While CpG methylation in the We generated Cidea-deficient mice and observed no upstream promoter region controls the production of obvious difference in cell death between wild-type and longer transcript, hepatocyte nuclear factor-4a (HNF4a) CideaÀ/À brown adipocytes. Surprisingly, CideaÀ/À mice binds to the internal promoter and controls the pro- showed a drastic lean phenotype with lower adiposity, duction of shorter transcripts of Cideb [20]. decreased leptin and plasma lipid levels and are resistant to diet-induced obesity. In particular, lipid content in On the posttranslational level, Cidea is degraded through CideaÀ/À mice is dramatically reduced upon cold treat- ubiquitin-mediated proteasome pathway in adipocytes ment, suggesting that Cidea is important in controlling [21]. Furthermore, Cidea was shown to be modified by energy expenditure in adipose tissues. In addition, O-linked glycosylation that may control its subcellular CideaÀ/À mice have higher glucose disposition rate and localization and cell death-inducing activity [22]. How- improved insulin sensitivity. The lean phenotype of ever, it remains to be determined if Cideb and Fsp27 are Cidea-null mice may be due to increased whole body controlled by similar posttranslational modifications. metabolism, higher basal lipolysis, and fatty acid oxi- dation in their brown adipocytes [36] (Table 1, Fig. 1). Subcellular localization of CIDE proteins The role of CIDE proteins in regulating metabolic dis- Much effort has been made toward subcellular localiz- orders was further confirmed in CidebÀ/À mice. Deficiency ation of the CIDE proteins. When overexpressed in of Cideb resulted in lower plasma triacylglycerol (TAG) and heterologous cells, Cidea and Cideb proteins showed a fatty acid levels, decreased white fat mass and increased distribution pattern similar to that of mitochondria whole body metabolism, and a lean phenotype [4,36]. specific marker – mitotracker [3,23]. Later, it was dis- In addition, CidebÀ/À mice are resistant to diet-induced covered that this particular pattern was associated specifi- obesity and liver steatosis. More interestingly, CidebÀ/À cally with the later stage of cell death. Recently, Cidea mice showed decreased plasma insulin concentration, was found to be localized to endoplasmic reticulum (ER) increased hepatic insulin sensitivity manifested by [24] and lipid droplet [25]. Similarly, Fsp27 targets increased IRS-1 and AKT2 phosphorylation in response to lipid droplets in adipocytes [5,26,27,28]. Lipid to insulin stimulation. The lean phenotype of CidebÀ/À droplets are highly dynamic organelles that are in close mice is likely due to a combination of increased fatty acid contact with multiple subcellular structures including ER, oxidation and decreased lipogenesis in CidebÀ/À hepato- endosomes, mitochondria, and plasma membrane [29]. cytes. Consistently, SREBP-1c, a crucial factor in regulat- Therefore, the discrepancy of these observations might ing fatty acid synthesis, was significantly downregulated, be due to the overexpression of proteins in heterologous resulting in the lower expression levels of its downstream cells that undergo specific morphological changes during target genes such as ACC1/2, fatty acid synthase (FAS), apoptosis or the diverse localization of lipid droplets. As and stearoyl-CoA desaturase (SCD) [4,36] (Table 1, nascent lipid droplet was proposed to be derived from the Fig. 2). The molecular mechanism by which Cideb con- cytosolic leaflet of ER [30], the ER and lipid droplet trols the expression levels of SREBP1c remains to be an localization of CIDE family proteins indicate their import- intensive area of future research. ant functions in lipid droplet formation. Fsp27À/À mice also have dramatically lower levels of TAG and much smaller lipid droplets in their white adipocytes CIDE proteins and the development of and are protected from diet-induced obesity. Fsp27À/À metabolic disorders mice also have higher glucose uptake rates and improved Due to their
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