Function and structure of lipid storage droplet protein 1 studied in lipoprotein complexes
Function and structure of lipid storage droplet protein 1 studied in lipoprotein complexes
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DOI：
10.1016/j.abb.2008.02.036
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发表时间：
2008-05-01
影响因子：
3.9
通讯作者：
Soulages, Jose L.
中科院分区：
文献类型：
--
作者：
Arrese, Estela L.;Rivera, Laticia;Soulages, Jose L.
储存在脂滴中的甘油三酯（TG）是所有动物的主要能量储备。动物动员TG的机制是复杂的，尚未完全了解。LD周围的几种蛋白质已经涉及TG稳态，如哺乳动物周脂蛋白A和昆虫脂质储存蛋白（Lsd）。大部分关于LD相关蛋白质的知识来自于使用细胞或LD的研究，这些蛋白质的生化特性未被表征。在这里，我们描述了重组Lsd 1的纯化和重建与脂质形成脂蛋白复合物的功能和结构的研究。Lsd 1在脂质结合状态下主要是α-螺旋蛋白。使用含有三油酸甘油酯的脂蛋白复合物，结果表明PKA介导的Lsd 1磷酸化促进了主要脂肪体脂肪酶的1.7倍活化，证明了Lsd I磷酸化和脂解活化之间的直接联系。丝氨酸20被确定为Lsd 1-磷酸化位点触发这种效应。(c)2008年爱思唯尔公司All rights reserved.
Triglycericles (TG) stored in lipid droplets (LDs) are the main energy reserve in all animals. The mechanism by which animals mobilize TG is complex and not fully understood. Several proteins surrounding the LDs have been implicated in TG homeostasis such as mammalian perilipin A and insect lipid storage proteins (Lsd). Most of the knowledge on LD-associated proteins comes from studies using cells or LDs leaving biochemical properties of these proteins uncharacterized. Here we describe the purification of recombinant Lsd1 and its reconstitution with lipids to form lipoprotein complexes suitable for functional and structural studies. Lsd1 in the lipid bound state is a predominately alpha-helical protein. Using lipoprotein complexes containing triolein it is shown that PKA mediated phosphorylation of Lsd1 promoted a 1.7-fold activation of the main fat body lipase demonstrating the direct link between Lsd I phosphorylation and activation of lipolysis. Serine 20 was identified as the Lsd1 -phosphorylation site triggering this effect. (c) 2008 Elsevier Inc. All rights reserved.