脂滴包被蛋白
磷酸化
脂滴
脂解
三烯丙基
生物化学
脂蛋白脂酶
化学
脂蛋白
丝氨酸
脂质代谢
细胞生物学
胆固醇
脂肪酶
生物
酶
脂肪组织
作者
Estela L. Arrese,Laticia Rivera,Masakazu Hamada,Saima Mirza,Steve Hartson,Susan T. Weintraub,José L. Soulages
标识
DOI:10.1016/j.abb.2008.02.036
摘要
Triglycerides (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 Lsd1 phosphorylation and activation of lipolysis. Serine 20 was identified as the Lsd1-phosphorylation site triggering this effect.
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