کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8303349 | 1537773 | 2010 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Identification of Yju3p as functional orthologue of mammalian monoglyceride lipase in the yeast Saccharomycescerevisiae
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کلمات کلیدی
FFADGATMGHmGlNAE2-AGmonoacylglycerolacyl-CoA:diacylglycerol acyltransferaseMAGMGATGFPN-acylphosphatidylethanolamineAEAendocannabinoid - آندوکانابینوئیدFree fatty acid - اسید چرب آزادtriacylglycerol - تری آسیل گلیسرول TAG یا triacylglycerols - تری گلیسرید یا تری آسیل گلیسرولdiacylglycerol - دیسیل گلیسیرینDAG - روزlipid droplet - قطره چربیmonoacylglycerol lipase - لیپاز monoacylglycerol لیپازMonoglyceride lipase - لیپاز مونوگلیسیریدYeast - مخمرMonoacylglycerols - مونوآسیلیک گلیسیرینNAPE - ناپاgreen fluorescent protein - پروتئین فلورسنت سبز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Identification of Yju3p as functional orthologue of mammalian monoglyceride lipase in the yeast Saccharomycescerevisiae Identification of Yju3p as functional orthologue of mammalian monoglyceride lipase in the yeast Saccharomycescerevisiae](/preview/png/8303349.png)
چکیده انگلیسی
Monoacylglycerols (MAGs) are short-lived intermediates of glycerolipid metabolism. Specific molecular species, such as 2-arachidonoylglycerol, which is a potent activator of cannabinoid receptors, may also function as lipid signaling molecules. In mammals, enzymes hydrolyzing MAG to glycerol and fatty acids, resembling the final step in lipolysis, or esterifying MAG to diacylglycerol, are well known; however, despite the high level of conservation of lipolysis, the corresponding activities in yeast have not been characterized yet. Here we provide evidence that the protein Yju3p functions as a potent MAG hydrolase in yeast. Cellular MAG hydrolase activity was decreased by more than 90% in extracts of Yju3p-deficient cells, indicating that Yju3p accounts for the vast majority of this activity in yeast. Loss of this activity was restored by heterologous expression of murine monoglyceride lipase (MGL). Since yju3Î mutants accumulated MAG in vivo only at very low concentrations, we considered the possibility that MAGs are re-esterified into DAG by acyltransferases. Indeed, cellular MAG levels were further increased in mutant cells lacking Yju3p and Dga1p or Lro1p acyltransferase activities. In conclusion, our studies suggest that catabolic and anabolic reactions affect cellular MAG levels. Yju3p is the functional orthologue of mammalian MGL and is required for efficient degradation of MAG in yeast.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1801, Issue 9, September 2010, Pages 1063-1071
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1801, Issue 9, September 2010, Pages 1063-1071
نویسندگان
Christoph Heier, Ulrike Taschler, Srinivasan Rengachari, Monika Oberer, Heimo Wolinski, Klaus Natter, Sepp D. Kohlwein, Regina Leber, Robert Zimmermann,