Abstract:
:The biogenesis of lipid droplets (LDs) and the development of adipocytes are two key aspects of mammalian fat storage. SEIPIN, an integral membrane protein of the endoplasmic reticulum (ER), plays a critical role in both LD formation and adipogenesis. The molecular function of SEIPIN, however, has yet to be elucidated. Here, we report the cryogenic electron microscopy structure of human SEIPIN at 3.8 Å resolution. SEIPIN exists as an undecamer, and this oligomerization state is critical for its physiological function. The evolutionarily conserved lumenal domain of SEIPIN forms an eight-stranded β sandwich fold. Both full-length SEIPIN and its lumenal domain can bind anionic phospholipids including phosphatidic acid. Our results suggest that SEIPIN forms a scaffold that helps maintain phospholipid homeostasis and surface tension of the ER.
journal_name
Dev Celljournal_title
Developmental cellauthors
Yan R,Qian H,Lukmantara I,Gao M,Du X,Yan N,Yang Hdoi
10.1016/j.devcel.2018.09.010subject
Has Abstractpub_date
2018-10-22 00:00:00pages
248-256.e4issue
2eissn
1534-5807issn
1878-1551pii
S1534-5807(18)30739-1journal_volume
47pub_type
杂志文章abstract::The myogenic regulatory genes Myf5, Mrf4, Myod, and Myogenin likely arose by gene duplications during evolution, presumably to address the more demanding requirements of the vertebrate body plan. Two cell lineages were proposed to be regulated independently by Myf5 and Myod to safeguard against tissue failure. Here we...
journal_title:Developmental cell
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journal_title:Developmental cell
pub_type: 杂志文章
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journal_title:Developmental cell
pub_type: 杂志文章
doi:10.1016/j.devcel.2016.02.010
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journal_title:Developmental cell
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