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)

Research output: Contribution to journalArticle

5 Downloads (Pure)

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 languageEnglish
Article number268
JournalCells
Volume8
Issue number3
Early online date21 Mar 2019
DOIs
Publication statusPublished - Mar 2019

Fingerprint

Congenital Generalized Lipodystrophy
Yeasts
Proteins
Fats
Pathology
Health
Lipid Droplets
Lipid Droplet Associated Proteins

Keywords

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

Cite this

Castro, I. G., Eisenberg-Bord, M., Persiani, E., Rochford, J. J., Schuldiner, M., & Bohnert, M. (2019). Promethin is a Conserved Seipin Partner Protein. Cells, 8(3), [268]. https://doi.org/10.3390/cells8030268

Promethin is a Conserved Seipin Partner Protein. / Castro, Inês G.; Eisenberg-Bord, Michal ; Persiani, Elisa; Rochford, Justin J. (Corresponding Author); Schuldiner, Maya (Corresponding Author); Bohnert, Maria (Corresponding Author).

In: Cells, Vol. 8, No. 3, 268, 03.2019.

Research output: Contribution to journalArticle

Castro, IG, Eisenberg-Bord, M, Persiani, E, Rochford, JJ, Schuldiner, M & Bohnert, M 2019, 'Promethin is a Conserved Seipin Partner Protein' Cells, vol. 8, no. 3, 268. https://doi.org/10.3390/cells8030268
Castro IG, Eisenberg-Bord M, Persiani E, Rochford JJ, Schuldiner M, Bohnert M. Promethin is a Conserved Seipin Partner Protein. Cells. 2019 Mar;8(3). 268. https://doi.org/10.3390/cells8030268
Castro, Inês G. ; Eisenberg-Bord, Michal ; Persiani, Elisa ; Rochford, Justin J. ; Schuldiner, Maya ; Bohnert, Maria . / Promethin is a Conserved Seipin Partner Protein. In: Cells. 2019 ; Vol. 8, No. 3.
@article{e369ebee05a54f13b74e30e06fe511b0,
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",
month = "3",
doi = "10.3390/cells8030268",
language = "English",
volume = "8",
journal = "Cells",
issn = "2073-4409",
publisher = "MDPI",
number = "3",

}

TY - JOUR

T1 - Promethin is a Conserved Seipin Partner Protein

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

Y1 - 2019/3

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.

KW - promethin

KW - TMEM159

KW - seipin

KW - BSCL2

KW - SPG17

KW - lipid droplets

KW - LD

KW - lipodystrophy

KW - LDO

KW - adipogenesis

KW - lipid droplet

KW - CONGENITAL LIPODYSTROPHY

KW - SIZE

KW - CHROMOSOME 11Q12-Q14

KW - IDENTIFICATION

KW - GENES

KW - BSCL2/SEIPIN

UR - http://www.mendeley.com/research/promethin-conserved-seipin-partner-protein

UR - https://abdn.pure.elsevier.com/en/en/researchoutput/promethin-is-a-conserved-seipin-partner-protein(e369ebee-05a5-4f13-b74e-30e06fe511b0).html

U2 - 10.3390/cells8030268

DO - 10.3390/cells8030268

M3 - Article

VL - 8

JO - Cells

JF - Cells

SN - 2073-4409

IS - 3

M1 - 268

ER -