Promethin is a Conserved Seipin Partner Protein

Inês G. Castro; Michal  Eisenberg-Bord; Elisa Persiani; Justin J. Rochford; Maya Schuldiner; Maria  Bohnert

doi:10.3390/cells8030268

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)

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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Abstract

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 language	English
Article number	268
Journal	Cells
Volume	8
Issue number	3
Early online date	21 Mar 2019
DOIs	https://doi.org/10.3390/cells8030268
Publication status	Published - Mar 2019

Bibliographical note

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.

Keywords

promethin
TMEM159
seipin
BSCL2
SPG17
lipid droplets
LD
lipodystrophy
LDO
adipogenesis
lipid droplet
CONGENITAL LIPODYSTROPHY
SIZE
CHROMOSOME 11Q12-Q14
IDENTIFICATION
GENES
BSCL2/SEIPIN

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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Promethin Is a Conserved Seipin Partner Protein
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0). https://creativecommons.org/licenses/by/4.0/
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Cite this

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title = "Promethin is a Conserved Seipin Partner Protein",

abstract = "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.",

keywords = "promethin, TMEM159, seipin, BSCL2, SPG17, lipid droplets, LD, lipodystrophy, LDO, adipogenesis, lipid droplet, CONGENITAL LIPODYSTROPHY, SIZE, CHROMOSOME 11Q12-Q14, IDENTIFICATION, GENES, BSCL2/SEIPIN",

author = "Castro, {In{\^e}s G.} and Michal Eisenberg-Bord and Elisa Persiani and Rochford, {Justin J.} and Maya Schuldiner and Maria Bohnert",

note = " The M.B. lab is supported by the Deutsche Forschungsgemeinschaft (DFG), Cells-in-Motion Cluster of Excellence (EXC 1003—CiM), University of M{\"u}nster, 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.",

year = "2019",

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doi = "10.3390/cells8030268",

language = "English",

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AU - Castro, Inês G.

AU - Eisenberg-Bord, Michal

AU - Persiani, Elisa

AU - Rochford, Justin J.

AU - Schuldiner, Maya

AU - Bohnert, Maria

N1 - 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

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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.

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KW - SPG17

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KW - adipogenesis

KW - lipid droplet

KW - CONGENITAL LIPODYSTROPHY

KW - SIZE

KW - CHROMOSOME 11Q12-Q14

KW - IDENTIFICATION

KW - GENES

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DO - 10.3390/cells8030268

M3 - Article

C2 - 30901948

SN - 2073-4409

VL - 8

JO - Cells

JF - Cells

IS - 3

M1 - 268

ER -

Promethin is a Conserved Seipin Partner Protein

Abstract

Bibliographical note

Keywords

UN SDGs

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