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Open AccessArticle

Promethin Is a Conserved Seipin Partner Protein

1
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel
2
Rowett Institute and Aberdeen Cardiovascular and Diabetes Centre, University of Aberdeen, Aberdeen AB25 2ZD, UK
3
Institute of Cell Dynamics and Imaging, University of Münster, Von-Esmarch-Str. 56, 48149 Münster, Germany
4
Cells-in-Motion Cluster of Excellence (EXC 1003—CiM), University of Münster, 48149 Münster, Germany
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Cells 2019, 8(3), 268; https://doi.org/10.3390/cells8030268
Received: 31 January 2019 / Revised: 3 March 2019 / Accepted: 14 March 2019 / Published: 21 March 2019
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. View Full-Text
Keywords: promethin; TMEM159; seipin; BSCL2; SPG17; lipid droplet; LD; lipodystrophy; LDO; adipogenesis promethin; TMEM159; seipin; BSCL2; SPG17; lipid droplet; LD; lipodystrophy; LDO; adipogenesis
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Castro, I.G.; Eisenberg-Bord, M.; Persiani, E.; Rochford, J.J.; Schuldiner, M.; Bohnert, M. Promethin Is a Conserved Seipin Partner Protein. Cells 2019, 8, 268.

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