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Seipin-still a mysterious protein?

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FRONTIERS MEDIA SA
DOI: 10.3389/fcell.2023.1112954

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seipin; lipid droplet; lipid droplet-ER contact sites; membrane contact site; endoplasmic reticulum; mitochondria-ER contact sites

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Cells store excess energy in lipid droplets (LDs), and the lipodystrophy protein seipin plays a crucial role in LD biogenesis and ER-LD contact site maintenance. Recent studies have provided insights into the molecular function of seipin as a LD nucleator in early LD biogenesis and its potential involvement in ER-mitochondria contact sites and calcium metabolism. This minireview discusses these recent findings.
Cells store excess energy in the form of lipid droplets (LDs), a specialized sub-compartment of the endoplasmic reticulum (ER) network. The lipodystrophy protein seipin is a key player in LD biogenesis and ER-LD contact site maintenance. Recent structural and in silico studies have started to shed light on the molecular function of seipin as a LD nucleator in early LD biogenesis, whilst new cell biological work implies a role for seipin in ER-mitochondria contact sites and calcium metabolism. In this minireview, I discuss recent insights into the molecular function of seipin.

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