文章基本信息

标题：Lipid droplet targeting domains of adipophilin
本地全文：下载
作者：James L. McManaman ; William Zabaronick ; Jerome Schaack 等
期刊名称：JLR Papers In Press
印刷版ISSN：0022-2275
电子版ISSN：1539-7262
出版年度：2003
卷号：44
期号：4
页码：668-673
DOI：10.1194/jlr.C200021-JLR200
语种：English
出版社：American Society for Biochemistry and Molecular Biology
摘要：Adipophilin (ADPH), a prominent protein component of lipid storage droplets (LSDs), is postulated to be necessary for the formation and cellular function of these structures. The presence of significant sequence similarities within an ∼100 amino acid region of the N-terminal portions of ADPH and related LSD binding proteins, perilipin and TIP47, has implicated this region, known as the “PAT” domain, in LSD targeting. Here we investigate the role of the PAT domain in targeting ADPH to LSDs by expressing this region, as well as selected N- and C-terminal truncations of mouse ADPH in COS 7 cells as epitope-tagged fusion proteins. Our studies show that truncations lacking either the PAT domain or the C-terminal half of ADPH both correctly targeted LSDs and increased the LSD content of transfected cells. Neither the PAT domain nor the C-terminal half of ADPH appeared to target LSDs or affect the LSD number. Instead, targeting fragments encompassed a putative α-helical region between amino acids 189 and 205, implicating this region in both LSD targeting and regulation of LSD formation.