Promethin Is a Conserved Seipin Partner Protein

Cells

Michal Eisenberg-Bord¹  InêsG. Castro¹  Maria Bohnert¹  Maya Schuldiner¹  Elisa Persiani²  JustinJ. Rochford² 

[1] Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel;Rowett Institute and Aberdeen Cardiovascular and Diabetes Centre, University of Aberdeen, Aberdeen AB25 2ZD, UK;

关键词: promethin;    TMEM159;    seipin;    BSCL2;    SPG17;    lipid droplet;    LD;    lipodystrophy;    LDO;    adipogenesis;   

DOI  :  10.3390/cells8030268

来源: DOAJ

【 摘 要 】

Seipin (BSCL2/SPG17) is a key factor in lipid droplet (LD) biology, and its dysfunction results in severe pathologies, including the fat storage disease Berardinelli-Seip congenital lipodystrophy type 2, as well as several neurological seipinopathies. Despite its importance for human health, the molecular role of seipin is still enigmatic. Seipin is evolutionarily conserved from yeast to humans. In yeast, seipin was recently found to cooperate with the lipid droplet organization (LDO) proteins, Ldo16 and Ldo45, two structurally-related proteins involved in LD function and identity that display remote homology to the human protein promethin/TMEM159. In this study, we show that promethin is indeed an LD-associated protein that forms a complex with seipin, and its localization to the LD surface can be modulated by seipin expression levels. We thus identify promethin as a novel seipin partner protein.

【 授权许可】

Unknown