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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 Rabdependent 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 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. Author links open overlay panel Veijo T. Add to Mendeley Share. Under an Elsevier user. Summary Seipin is an oligomeric integral endoplasmic reticulum ER protein involved in lipid droplet LD biogenesis.
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