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Perilipins: a diversity of intracellular lipid droplet proteins

Intracellular lipid droplets (LDs) are found in a wide variety of cell types and have been recognized as organelles with unique spherical structures. Although LDs are not stable lipid-depots, they are active sites of neutral lipid metabolism, and comprise neutral lipid or cholesterol cores surrounde...

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Autores principales: Itabe, Hiroyuki, Yamaguchi, Tomohiro, Nimura, Satomi, Sasabe, Naoko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5410086/
https://www.ncbi.nlm.nih.gov/pubmed/28454542
http://dx.doi.org/10.1186/s12944-017-0473-y
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author Itabe, Hiroyuki
Yamaguchi, Tomohiro
Nimura, Satomi
Sasabe, Naoko
author_facet Itabe, Hiroyuki
Yamaguchi, Tomohiro
Nimura, Satomi
Sasabe, Naoko
author_sort Itabe, Hiroyuki
collection PubMed
description Intracellular lipid droplets (LDs) are found in a wide variety of cell types and have been recognized as organelles with unique spherical structures. Although LDs are not stable lipid-depots, they are active sites of neutral lipid metabolism, and comprise neutral lipid or cholesterol cores surrounded by phospholipid monolayers containing specialized proteins. However, sizes and protein compositions vary between cell and tissue types. Proteins of the perilipin family have been associated with surfaces of LDs and all carry a conserved 11-mer repeat motif. Accumulating evidence indicates that all perilipins are involved in LD formation and that all play roles in LD function under differing conditions. In this brief review, we summarize current knowledge of the roles of perilipins and lipid metabolizing enzymes in a variety of mammalian cell types.
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spelling pubmed-54100862017-05-02 Perilipins: a diversity of intracellular lipid droplet proteins Itabe, Hiroyuki Yamaguchi, Tomohiro Nimura, Satomi Sasabe, Naoko Lipids Health Dis Review Intracellular lipid droplets (LDs) are found in a wide variety of cell types and have been recognized as organelles with unique spherical structures. Although LDs are not stable lipid-depots, they are active sites of neutral lipid metabolism, and comprise neutral lipid or cholesterol cores surrounded by phospholipid monolayers containing specialized proteins. However, sizes and protein compositions vary between cell and tissue types. Proteins of the perilipin family have been associated with surfaces of LDs and all carry a conserved 11-mer repeat motif. Accumulating evidence indicates that all perilipins are involved in LD formation and that all play roles in LD function under differing conditions. In this brief review, we summarize current knowledge of the roles of perilipins and lipid metabolizing enzymes in a variety of mammalian cell types. BioMed Central 2017-04-28 /pmc/articles/PMC5410086/ /pubmed/28454542 http://dx.doi.org/10.1186/s12944-017-0473-y Text en © The Author(s). 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Review
Itabe, Hiroyuki
Yamaguchi, Tomohiro
Nimura, Satomi
Sasabe, Naoko
Perilipins: a diversity of intracellular lipid droplet proteins
title Perilipins: a diversity of intracellular lipid droplet proteins
title_full Perilipins: a diversity of intracellular lipid droplet proteins
title_fullStr Perilipins: a diversity of intracellular lipid droplet proteins
title_full_unstemmed Perilipins: a diversity of intracellular lipid droplet proteins
title_short Perilipins: a diversity of intracellular lipid droplet proteins
title_sort perilipins: a diversity of intracellular lipid droplet proteins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5410086/
https://www.ncbi.nlm.nih.gov/pubmed/28454542
http://dx.doi.org/10.1186/s12944-017-0473-y
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