Cargando…

Seipin forms a flexible cage at lipid droplet formation sites

Lipid droplets (LDs) form in the endoplasmic reticulum by phase separation of neutral lipids. This process is facilitated by the seipin protein complex, which consists of a ring of seipin monomers, with a yet unclear function. Here, we report a structure of S. cerevisiae seipin based on cryogenic-el...

Descripción completa

Detalles Bibliográficos
Autores principales: Arlt, Henning, Sui, Xuewu, Folger, Brayden, Adams, Carson, Chen, Xiao, Remme, Roman, Hamprecht, Fred A., DiMaio, Frank, Liao, Maofu, Goodman, Joel M., Farese, Robert V., Walther, Tobias C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group US 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8930772/
https://www.ncbi.nlm.nih.gov/pubmed/35210614
http://dx.doi.org/10.1038/s41594-021-00718-y
_version_ 1784671111216103424
author Arlt, Henning
Sui, Xuewu
Folger, Brayden
Adams, Carson
Chen, Xiao
Remme, Roman
Hamprecht, Fred A.
DiMaio, Frank
Liao, Maofu
Goodman, Joel M.
Farese, Robert V.
Walther, Tobias C.
author_facet Arlt, Henning
Sui, Xuewu
Folger, Brayden
Adams, Carson
Chen, Xiao
Remme, Roman
Hamprecht, Fred A.
DiMaio, Frank
Liao, Maofu
Goodman, Joel M.
Farese, Robert V.
Walther, Tobias C.
author_sort Arlt, Henning
collection PubMed
description Lipid droplets (LDs) form in the endoplasmic reticulum by phase separation of neutral lipids. This process is facilitated by the seipin protein complex, which consists of a ring of seipin monomers, with a yet unclear function. Here, we report a structure of S. cerevisiae seipin based on cryogenic-electron microscopy and structural modeling data. Seipin forms a decameric, cage-like structure with the lumenal domains forming a stable ring at the cage floor and transmembrane segments forming the cage sides and top. The transmembrane segments interact with adjacent monomers in two distinct, alternating conformations. These conformations result from changes in switch regions, located between the lumenal domains and the transmembrane segments, that are required for seipin function. Our data indicate a model for LD formation in which a closed seipin cage enables triacylglycerol phase separation and subsequently switches to an open conformation to allow LD growth and budding.
format Online
Article
Text
id pubmed-8930772
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Nature Publishing Group US
record_format MEDLINE/PubMed
spelling pubmed-89307722022-03-23 Seipin forms a flexible cage at lipid droplet formation sites Arlt, Henning Sui, Xuewu Folger, Brayden Adams, Carson Chen, Xiao Remme, Roman Hamprecht, Fred A. DiMaio, Frank Liao, Maofu Goodman, Joel M. Farese, Robert V. Walther, Tobias C. Nat Struct Mol Biol Article Lipid droplets (LDs) form in the endoplasmic reticulum by phase separation of neutral lipids. This process is facilitated by the seipin protein complex, which consists of a ring of seipin monomers, with a yet unclear function. Here, we report a structure of S. cerevisiae seipin based on cryogenic-electron microscopy and structural modeling data. Seipin forms a decameric, cage-like structure with the lumenal domains forming a stable ring at the cage floor and transmembrane segments forming the cage sides and top. The transmembrane segments interact with adjacent monomers in two distinct, alternating conformations. These conformations result from changes in switch regions, located between the lumenal domains and the transmembrane segments, that are required for seipin function. Our data indicate a model for LD formation in which a closed seipin cage enables triacylglycerol phase separation and subsequently switches to an open conformation to allow LD growth and budding. Nature Publishing Group US 2022-02-24 2022 /pmc/articles/PMC8930772/ /pubmed/35210614 http://dx.doi.org/10.1038/s41594-021-00718-y Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Arlt, Henning
Sui, Xuewu
Folger, Brayden
Adams, Carson
Chen, Xiao
Remme, Roman
Hamprecht, Fred A.
DiMaio, Frank
Liao, Maofu
Goodman, Joel M.
Farese, Robert V.
Walther, Tobias C.
Seipin forms a flexible cage at lipid droplet formation sites
title Seipin forms a flexible cage at lipid droplet formation sites
title_full Seipin forms a flexible cage at lipid droplet formation sites
title_fullStr Seipin forms a flexible cage at lipid droplet formation sites
title_full_unstemmed Seipin forms a flexible cage at lipid droplet formation sites
title_short Seipin forms a flexible cage at lipid droplet formation sites
title_sort seipin forms a flexible cage at lipid droplet formation sites
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8930772/
https://www.ncbi.nlm.nih.gov/pubmed/35210614
http://dx.doi.org/10.1038/s41594-021-00718-y
work_keys_str_mv AT arlthenning seipinformsaflexiblecageatlipiddropletformationsites
AT suixuewu seipinformsaflexiblecageatlipiddropletformationsites
AT folgerbrayden seipinformsaflexiblecageatlipiddropletformationsites
AT adamscarson seipinformsaflexiblecageatlipiddropletformationsites
AT chenxiao seipinformsaflexiblecageatlipiddropletformationsites
AT remmeroman seipinformsaflexiblecageatlipiddropletformationsites
AT hamprechtfreda seipinformsaflexiblecageatlipiddropletformationsites
AT dimaiofrank seipinformsaflexiblecageatlipiddropletformationsites
AT liaomaofu seipinformsaflexiblecageatlipiddropletformationsites
AT goodmanjoelm seipinformsaflexiblecageatlipiddropletformationsites
AT fareserobertv seipinformsaflexiblecageatlipiddropletformationsites
AT walthertobiasc seipinformsaflexiblecageatlipiddropletformationsites