TY - JOUR
T1 - Promethin Is a Conserved Seipin Partner Protein
AU - Castro, Ines G.
AU - Eisenberg-Bord, Michal
AU - Persiani, Elisa
AU - Rochford, Justin J.
AU - Schuldiner, Maya
AU - Bohnert, Maria
N1 - Acknowledgments: We would like to thank Pedro Carvalho for the Sei1 and Ldb16 antibodies, Yoav Peleg from the Dana and Yossie Hollander Center for Structural Proteomics for help with cloning, and all members of our groups for stimulating discussions. Funding: The M.B. lab is supported by the Deutsche Forschungsgemeinschaft (DFG), Cells-in-Motion Cluster of Excellence (EXC 1003—CiM), University of Münster, Germany. The M.S. lab is funded by an SFB1190 by the DFG and a Volkswagen Stiftung “Life” Grant (93092). M.S. is an Incumbent of the Dr. Gilbert Omenn and Martha Darling Professorial Chair in Molecular Genetics. The J.J.R. lab is supported the Medical Research Council [Research Grant MR/L002620/1] and the Biotechnology and Biological Sciences Research Council [BB/K017772/1]. I.G.C. is supported by an EMBO Long-term Fellowship (ALTF-580-2017). M.E.B. is grateful to the Azrieli Foundation for the award of an Azrieli Fellowship.
PY - 2019/3/21
Y1 - 2019/3/21
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85064977125&partnerID=8YFLogxK
U2 - 10.3390/cells8030268
DO - 10.3390/cells8030268
M3 - مقالة
SN - 2073-4409
VL - 8
JO - Cells
JF - Cells
IS - 3
M1 - 268
ER -