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      SCD1 promotes lipid mobilization in subcutaneous white adipose tissue

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          Abstract

          Beiging of white adipose tissue (WAT) has beneficial effects on metabolism. Although it is known that beige adipocytes are active in lipid catabolism and thermogenesis, how they are regulated deserves more explorations. In this study, we demonstrate that stearoyl-CoA desaturase 1 (SCD1) in subcutaneous WAT (scWAT) responded to cold stimulation and was able to promote mobilization of triacylglycerol [TAG (triglyceride)]. In vitro studies showed that SCD1 promoted lipolysis in C3H10T1/2 white adipocytes. The lipolytic effect was contributed by one of SCD1’s products, oleic acid (OA). OA upregulated adipose TAG lipase and hormone-sensitive lipase expression. When SCD1 was overexpressed in the scWAT of mice, lipolysis was enhanced, and oxygen consumption and heat generation were increased. These effects were also demonstrated by the SCD1 knockdown experiments in mice. In conclusion, our study suggests that SCD1, known as an enzyme for lipid synthesis, plays a role in upregulating lipid mobilization through its desaturation product, OA.

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          p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy.

          Serhiy Pankiv, Terje Clausen, Trond Lamark … (2007)
          Protein degradation by basal constitutive autophagy is important to avoid accumulation of polyubiquitinated protein aggregates and development of neurodegenerative diseases. The polyubiquitin-binding protein p62/SQSTM1 is degraded by autophagy. It is found in cellular inclusion bodies together with polyubiquitinated proteins and in cytosolic protein aggregates that accumulate in various chronic, toxic, and degenerative diseases. Here we show for the first time a direct interaction between p62 and the autophagic effector proteins LC3A and -B and the related gamma-aminobutyrate receptor-associated protein and gamma-aminobutyrate receptor-associated-like proteins. The binding is mediated by a 22-residue sequence of p62 containing an evolutionarily conserved motif. To monitor the autophagic sequestration of p62- and LC3-positive bodies, we developed a novel pH-sensitive fluorescent tag consisting of a tandem fusion of the red, acid-insensitive mCherry and the acid-sensitive green fluorescent proteins. This approach revealed that p62- and LC3-positive bodies are degraded in autolysosomes. Strikingly, even rather large p62-positive inclusion bodies (2 microm diameter) become degraded by autophagy. The specific interaction between p62 and LC3, requiring the motif we have mapped, is instrumental in mediating autophagic degradation of the p62-positive bodies. We also demonstrate that the previously reported aggresome-like induced structures containing ubiquitinated proteins in cytosolic bodies are dependent on p62 for their formation. In fact, p62 bodies and these structures are indistinguishable. Taken together, our results clearly suggest that p62 is required both for the formation and the degradation of polyubiquitin-containing bodies by autophagy.
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            Autophagy regulates lipid metabolism.

            Rajat Singh, Susmita Kaushik, Yongjun Wang … (2009)
            The intracellular storage and utilization of lipids are critical to maintain cellular energy homeostasis. During nutrient deprivation, cellular lipids stored as triglycerides in lipid droplets are hydrolysed into fatty acids for energy. A second cellular response to starvation is the induction of autophagy, which delivers intracellular proteins and organelles sequestered in double-membrane vesicles (autophagosomes) to lysosomes for degradation and use as an energy source. Lipolysis and autophagy share similarities in regulation and function but are not known to be interrelated. Here we show a previously unknown function for autophagy in regulating intracellular lipid stores (macrolipophagy). Lipid droplets and autophagic components associated during nutrient deprivation, and inhibition of autophagy in cultured hepatocytes and mouse liver increased triglyceride storage in lipid droplets. This study identifies a critical function for autophagy in lipid metabolism that could have important implications for human diseases with lipid over-accumulation such as those that comprise the metabolic syndrome.
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              A creatine-driven substrate cycle enhances energy expenditure and thermogenesis in beige fat.

              Lawrence Kazak, Edward Chouchani, Mark P. Jedrychowski … (2015)
              Thermogenic brown and beige adipose tissues dissipate chemical energy as heat, and their thermogenic activities can combat obesity and diabetes. Herein the functional adaptations to cold of brown and beige adipose depots are examined using quantitative mitochondrial proteomics. We identify arginine/creatine metabolism as a beige adipose signature and demonstrate that creatine enhances respiration in beige-fat mitochondria when ADP is limiting. In murine beige fat, cold exposure stimulates mitochondrial creatine kinase activity and induces coordinated expression of genes associated with creatine metabolism. Pharmacological reduction of creatine levels decreases whole-body energy expenditure after administration of a β3-agonist and reduces beige and brown adipose metabolic rate. Genes of creatine metabolism are compensatorily induced when UCP1-dependent thermogenesis is ablated, and creatine reduction in Ucp1-deficient mice reduces core body temperature. These findings link a futile cycle of creatine metabolism to adipose tissue energy expenditure and thermal homeostasis. PAPERCLIP.
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Lipid Res
                Journal ID (iso-abbrev): J Lipid Res
                Journal ID (hwp): jlr
                Journal ID (pmc): jlr
                Journal ID (publisher-id): jlr
                Title: Journal of Lipid Research
                Publisher: The American Society for Biochemistry and Molecular Biology
                ISSN (Print): 0022-2275
                ISSN (Electronic): 1539-7262
                Publication date (Print): December 2020
                Publication date (Electronic): 25 September 2020
                Publication date PMC-release: 25 September 2020
                Volume: 61
                Issue: 12
                Pages: 1589-1604
                Affiliations
                [1 ]Key Laboratory of Metabolism and Molecular Medicine, Ministry of Education, Department of Biochemistry and Molecular Biology of the School of Basic Medical Sciences, and Department of Endocrinology and Metabolism of Zhongshan Hospital, Fudan University , Shanghai Medical College, Shanghai, China
                [2 ]Key Laboratory of Metabolism and Molecular Medicine, Ministry of Education, Institutes of Biomedical Sciences, Fudan University , Shanghai, China
                Author notes
                [‡]

                These authors contributed equally to the work.

                [* ]For correspondence: Qi-Qun Tang, qqtang@ 123456shmu.edu.cn ; Shu-Wen Qian, shuwenqian2013@ 123456163.com .
                Article
                Publisher ID: rA120000869
                DOI: 10.1194/jlr.RA120000869
                PMC ID: 7707166
                PubMed ID: 32978274
                SO-VID: 4b7b6e6a-d73d-4662-9794-6aea604a4549
                Copyright © Copyright © 2020 Zou et al. Published by The American Society for Biochemistry and Molecular Biology, Inc.
                License:

                Author’s Choice—Final version open access under the terms of the Creative Commons CC-BY license.

                History
                Funding
                Funded by: National Natural Science Foundation of China, open-funder-registry 10.13039/501100001809;
                Award ID: 81730021
                Award ID: 31670787
                Award ID: 81200621
                Award ID: 81970754
                Categories
                Subject: Research Articles

                ScienceOpen disciplines: Biochemistry
                Keywords: stearoyl-coa desaturase-1,triacylglycerol,adipocytes,lipolysis,lipophagy,oleic acid,thermogenesis
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: stearoyl-coa desaturase-1, triacylglycerol, adipocytes, lipolysis, lipophagy, oleic acid, thermogenesis

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