The human lipodystrophy protein seipin is an ER membrane adaptor for the adipogenic PA phosphatase lipin 1

M. F.Michelle Sim, Rowena J. Dennis, Evelyne M. Aubry, Nardev Ramanathan, Hiroshi Sembongi, Vladimir Saudek, Daisuke Ito, Stephen O'Rahilly, Symeon Siniossoglou, Justin J. Rochford

研究成果: Article査読

61 被引用数 (Scopus)

抄録

Disruption of the gene BSCL2 causes a severe, generalised lipodystrophy, demonstrating the critical role of its protein product, seipin, in human adipose tissue development. Seipin is essential for adipocyte differentiation, whilst the study of seipin in non-adipose cells has suggested a role in lipid droplet formation. However, its precise molecular function remains poorly understood. Here we demonstrate that seipin can inducibly bind lipin 1, a phosphatidic acid (PA) phosphatase important for lipid synthesis and adipogenesis. Knockdown of seipin during early adipogenesis decreases the association of lipin 1 with membranes and increases the accumulation of its substrate PA. Conversely, PA levels are reduced in differentiating cells by overexpression of wild-type seipin but not by expression of a mutated seipin that is unable to bind lipin 1. Together our data identify lipin as the first example of a seipin-interacting protein and reveals a novel molecular function for seipin in developing adipocytes.

本文言語English
ページ(範囲)38-46
ページ数9
ジャーナルMolecular Metabolism
2
1
DOI
出版ステータスPublished - 2013 2月

ASJC Scopus subject areas

  • 分子生物学
  • 細胞生物学

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