Seipin—still a mysterious protein?

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 l...

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Detalles Bibliográficos
Autor principal: Salo, Veijo T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Cell and Developmental Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9935593/
https://www.ncbi.nlm.nih.gov/pubmed/36819093
http://dx.doi.org/10.3389/fcell.2023.1112954
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author Salo, Veijo T.
author_facet Salo, Veijo T.
author_sort Salo, Veijo T.
collection PubMed
description 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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spelling pubmed-99355932023-02-18 Seipin—still a mysterious protein? Salo, Veijo T. Front Cell Dev Biol Cell and Developmental Biology 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. Frontiers Media S.A. 2023-02-03 /pmc/articles/PMC9935593/ /pubmed/36819093 http://dx.doi.org/10.3389/fcell.2023.1112954 Text en Copyright © 2023 Salo. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Cell and Developmental Biology
Salo, Veijo T.
Seipin—still a mysterious protein?
title Seipin—still a mysterious protein?
title_full Seipin—still a mysterious protein?
title_fullStr Seipin—still a mysterious protein?
title_full_unstemmed Seipin—still a mysterious protein?
title_short Seipin—still a mysterious protein?
title_sort seipin—still a mysterious protein?
topic Cell and Developmental Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9935593/
https://www.ncbi.nlm.nih.gov/pubmed/36819093
http://dx.doi.org/10.3389/fcell.2023.1112954
work_keys_str_mv AT saloveijot seipinstillamysteriousprotein

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