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脂肪酸结合蛋白与比较基因识别-58相互作用，将脂肪分解与脂质配体穿梭联系起来。

Fatty Acid-binding Proteins Interact with Comparative Gene Identification-58 Linking Lipolysis with Lipid Ligand Shuttling.

作者信息

Hofer Peter, Boeszoermenyi Andras, Jaeger Doris, Feiler Ursula, Arthanari Haribabu, Mayer Nicole, Zehender Fabian, Rechberger Gerald, Oberer Monika, Zimmermann Robert, Lass Achim, Haemmerle Guenter, Breinbauer Rolf, Zechner Rudolf, Preiss-Landl Karina

机构信息

From the Institute of Molecular Biosciences, University of Graz, NAWI Graz, 8010 Graz, Austria.

the Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.

出版信息

J Biol Chem. 2015 Jul 24;290(30):18438-53. doi: 10.1074/jbc.M114.628958. Epub 2015 May 7.

DOI:10.1074/jbc.M114.628958
PMID:25953897
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4513104/
Abstract

The coordinated breakdown of intracellular triglyceride (TG) stores requires the exquisitely regulated interaction of lipolytic enzymes with regulatory, accessory, and scaffolding proteins. Together they form a dynamic multiprotein network designated as the "lipolysome." Adipose triglyceride lipase (Atgl) catalyzes the initiating step of TG hydrolysis and requires comparative gene identification-58 (Cgi-58) as a potent activator of enzyme activity. Here, we identify adipocyte-type fatty acid-binding protein (A-Fabp) and other members of the fatty acid-binding protein (Fabp) family as interaction partners of Cgi-58. Co-immunoprecipitation, microscale thermophoresis, and solid phase assays proved direct protein/protein interaction between A-Fabp and Cgi-58. Using nuclear magnetic resonance titration experiments and site-directed mutagenesis, we located a potential contact region on A-Fabp. In functional terms, A-Fabp stimulates Atgl-catalyzed TG hydrolysis in a Cgi-58-dependent manner. Additionally, transcriptional transactivation assays with a luciferase reporter system revealed that Fabps enhance the ability of Atgl/Cgi-58-mediated lipolysis to induce the activity of peroxisome proliferator-activated receptors. Our studies identify Fabps as crucial structural and functional components of the lipolysome.

摘要

细胞内甘油三酯（TG）储存的协同分解需要脂解酶与调节、辅助和支架蛋白之间进行精确调控的相互作用。它们共同形成了一个动态的多蛋白网络，称为“脂解小体”。脂肪甘油三酯脂肪酶（Atgl）催化TG水解的起始步骤，并且需要比较基因识别-58（Cgi-58）作为酶活性的有效激活剂。在此，我们鉴定出脂肪细胞型脂肪酸结合蛋白（A-Fabp）以及脂肪酸结合蛋白（Fabp）家族的其他成员为Cgi-58的相互作用伙伴。免疫共沉淀、微量热泳动和固相分析证明了A-Fabp与Cgi-58之间存在直接的蛋白质/蛋白质相互作用。通过核磁共振滴定实验和定点诱变，我们在A-Fabp上定位了一个潜在的接触区域。在功能方面，A-Fabp以Cgi-58依赖的方式刺激Atgl催化的TG水解。此外，使用荧光素酶报告系统进行的转录反式激活分析表明，Fabps增强了Atgl/Cgi-58介导的脂解作用诱导过氧化物酶体增殖物激活受体活性的能力。我们的研究将Fabps鉴定为脂解小体的关键结构和功能成分。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5428/4513104/e5e473a3df73/zbc0301519530008.jpg
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