Seipin Facilitates Triglyceride Flow to Lipid Droplet and Counteracts Droplet Ripening via Endoplasmic Reticulum Contact

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Salo , V T , Li , S , Vihinen , H , Hölttä-Vuori , M , Szkalisity , A , Horvath , P , Belevich , I , Peränen , J , Thiele , C , Somerharju , P , Zhao , H , Santinho , A , Thiam , A R , Jokitalo , E & Ikonen , E 2019 , ' Seipin Facilitates Triglyceride Flow to Lipid Droplet and Counteracts Droplet Ripening via Endoplasmic Reticulum Contact ' , Developmental Cell , vol. 50 , no. 4 , pp. 478-+ . https://doi.org/10.1016/j.devcel.2019.05.016

Title: Seipin Facilitates Triglyceride Flow to Lipid Droplet and Counteracts Droplet Ripening via Endoplasmic Reticulum Contact
Author: Salo, Veijo T.; Li, Shiqian; Vihinen, Helena; Hölttä-Vuori, Maarit; Szkalisity, Abel; Horvath, Peter; Belevich, Ilya; Peränen, Johan; Thiele, Christoph; Somerharju, Pentti; Zhao, Hongxia; Santinho, Alexandre; Thiam, Abdou Rachid; Jokitalo, Eija; Ikonen, Elina
Contributor: University of Helsinki, Department of Anatomy
University of Helsinki, Department of Anatomy
University of Helsinki, Institute of Biotechnology
University of Helsinki, University Management
University of Helsinki, Biological Research Center of Hungarian Academy of Sciences
University of Helsinki, Electron Microscopy
University of Helsinki, University Management
University of Helsinki, University Management
University of Helsinki, Hongxia Zhao / Principal Investigator
University of Helsinki, University Management
University of Helsinki, Lipid Trafficking Lab
Date: 2019-08-19
Language: eng
Number of pages: 25
Belongs to series: Developmental Cell
ISSN: 1534-5807
URI: http://hdl.handle.net/10138/312959
Abstract: Seipin is an oligomeric integral endoplasmic reticulum (ER) protein involved in lipid droplet (LD) biogenesis. To study the role of seipin in LD formation, we relocalized it to the nuclear envelope and found that LDs formed at these new seipin-defined sites. The sites were characterized by uniform seipin-mediated ER-LD necks. At low seipin content, LDs only grew at seipin sites, and tiny, growth-incompetent LDs appeared in a Rab18-dependent manner. When seipin was removed from ER-LD contacts within 1 h, no lipid metabolic defects were observed, but LDs became heterogeneous in size. Studies in seipin-ablated cells and model membranes revealed that this heterogeneity arises via a biophysical ripening process, with triglycerides partitioning from smaller to larger LDs through droplet-bilayer contacts. These results suggest that seipin supports the formation of structurally uniform ER-LD contacts and facilitates the delivery of triglycerides from ER to LDs. This counteracts ripening-induced shrinkage of small LDs.
Subject: CONGENITAL LIPODYSTROPHY
PHOSPHATIDIC-ACID
ER
PROTEINS
BIOGENESIS
GROWTH
CELLS
RAB18
PHOSPHOLIPIDS
ACCUMULATION
3111 Biomedicine
1182 Biochemistry, cell and molecular biology
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