COPI complex is a regulator of lipid homeostasis.

Lipid droplets are ubiquitous triglyceride and sterol ester storage organelles required for energy storage homeostasis and biosynthesis. Although little is known about lipid droplet formation and regulation, it is clear that members of the PAT (perilipin, adipocyte differentiation related protein, t...

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Autores principales:	Mathias Beller, Carole Sztalryd, Noel Southall, Ming Bell, Herbert Jäckle, Douglas S Auld, Brian Oliver
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2008
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/1c3a028d110a46349c12324d1336a22f
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spelling	oai:doaj.org-article:1c3a028d110a46349c12324d1336a22f2021-11-25T05:33:55ZCOPI complex is a regulator of lipid homeostasis.1544-91731545-788510.1371/journal.pbio.0060292https://doaj.org/article/1c3a028d110a46349c12324d1336a22f2008-11-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19067489/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Lipid droplets are ubiquitous triglyceride and sterol ester storage organelles required for energy storage homeostasis and biosynthesis. Although little is known about lipid droplet formation and regulation, it is clear that members of the PAT (perilipin, adipocyte differentiation related protein, tail interacting protein of 47 kDa) protein family coat the droplet surface and mediate interactions with lipases that remobilize the stored lipids. We identified key Drosophila candidate genes for lipid droplet regulation by RNA interference (RNAi) screening with an image segmentation-based optical read-out system, and show that these regulatory functions are conserved in the mouse. Those include the vesicle-mediated Coat Protein Complex I (COPI) transport complex, which is required for limiting lipid storage. We found that COPI components regulate the PAT protein composition at the lipid droplet surface, and promote the association of adipocyte triglyceride lipase (ATGL) with the lipid droplet surface to mediate lipolysis. Two compounds known to inhibit COPI function, Exo1 and Brefeldin A, phenocopy COPI knockdowns. Furthermore, RNAi inhibition of ATGL and simultaneous drug treatment indicate that COPI and ATGL function in the same pathway. These data indicate that the COPI complex is an evolutionarily conserved regulator of lipid homeostasis, and highlight an interaction between vesicle transport systems and lipid droplets.Mathias BellerCarole SztalrydNoel SouthallMing BellHerbert JäckleDouglas S AuldBrian OliverPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 6, Iss 11, p e292 (2008)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Mathias Beller Carole Sztalryd Noel Southall Ming Bell Herbert Jäckle Douglas S Auld Brian Oliver COPI complex is a regulator of lipid homeostasis.
description	Lipid droplets are ubiquitous triglyceride and sterol ester storage organelles required for energy storage homeostasis and biosynthesis. Although little is known about lipid droplet formation and regulation, it is clear that members of the PAT (perilipin, adipocyte differentiation related protein, tail interacting protein of 47 kDa) protein family coat the droplet surface and mediate interactions with lipases that remobilize the stored lipids. We identified key Drosophila candidate genes for lipid droplet regulation by RNA interference (RNAi) screening with an image segmentation-based optical read-out system, and show that these regulatory functions are conserved in the mouse. Those include the vesicle-mediated Coat Protein Complex I (COPI) transport complex, which is required for limiting lipid storage. We found that COPI components regulate the PAT protein composition at the lipid droplet surface, and promote the association of adipocyte triglyceride lipase (ATGL) with the lipid droplet surface to mediate lipolysis. Two compounds known to inhibit COPI function, Exo1 and Brefeldin A, phenocopy COPI knockdowns. Furthermore, RNAi inhibition of ATGL and simultaneous drug treatment indicate that COPI and ATGL function in the same pathway. These data indicate that the COPI complex is an evolutionarily conserved regulator of lipid homeostasis, and highlight an interaction between vesicle transport systems and lipid droplets.
format	article
author	Mathias Beller Carole Sztalryd Noel Southall Ming Bell Herbert Jäckle Douglas S Auld Brian Oliver
author_facet	Mathias Beller Carole Sztalryd Noel Southall Ming Bell Herbert Jäckle Douglas S Auld Brian Oliver
author_sort	Mathias Beller
title	COPI complex is a regulator of lipid homeostasis.
title_short	COPI complex is a regulator of lipid homeostasis.
title_full	COPI complex is a regulator of lipid homeostasis.
title_fullStr	COPI complex is a regulator of lipid homeostasis.
title_full_unstemmed	COPI complex is a regulator of lipid homeostasis.
title_sort	copi complex is a regulator of lipid homeostasis.
publisher	Public Library of Science (PLoS)
publishDate	2008
url	https://doaj.org/article/1c3a028d110a46349c12324d1336a22f
work_keys_str_mv	AT mathiasbeller copicomplexisaregulatoroflipidhomeostasis AT carolesztalryd copicomplexisaregulatoroflipidhomeostasis AT noelsouthall copicomplexisaregulatoroflipidhomeostasis AT mingbell copicomplexisaregulatoroflipidhomeostasis AT herbertjackle copicomplexisaregulatoroflipidhomeostasis AT douglassauld copicomplexisaregulatoroflipidhomeostasis AT brianoliver copicomplexisaregulatoroflipidhomeostasis
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COPI complex is a regulator of lipid homeostasis.

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