Promethin is a Conserved Seipin Partner Protein

Inês G. Castro, Michal Eisenberg-Bord, Elisa Persiani, Justin J. Rochford (Corresponding Author), Maya Schuldiner (Corresponding Author), Maria Bohnert (Corresponding Author)

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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.
Original languageEnglish
Article number268
Issue number3
Early online date21 Mar 2019
Publication statusPublished - Mar 2019


  • promethin
  • TMEM159
  • seipin
  • BSCL2
  • SPG17
  • lipid droplets
  • LD
  • lipodystrophy
  • LDO
  • adipogenesis
  • lipid droplet
  • SIZE
  • CHROMOSOME 11Q12-Q14


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