Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes

Perilipin 1 is a lipid droplet coating protein known to regulate lipid metabolism in adipocytes by serving as a physical barrier as well as a recruitment site for lipases to the lipid droplet. Phosphorylation of perilipin 1 by protein kinase A rapidly initiates lipolysis, but the detailed mechanism...

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Main Authors: Hansen, J, De Maré, S, Jones, H, Göransson, O, Lindkvist-Petersson, K
Format: Journal article
Language:English
Published: Springer Nature 2017
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author Hansen, J
De Maré, S
Jones, H
Göransson, O
Lindkvist-Petersson, K
author_facet Hansen, J
De Maré, S
Jones, H
Göransson, O
Lindkvist-Petersson, K
author_sort Hansen, J
collection OXFORD
description Perilipin 1 is a lipid droplet coating protein known to regulate lipid metabolism in adipocytes by serving as a physical barrier as well as a recruitment site for lipases to the lipid droplet. Phosphorylation of perilipin 1 by protein kinase A rapidly initiates lipolysis, but the detailed mechanism on how perilipin 1 controls lipolysis is unknown. Here, we identify specific lipid binding properties of perilipin 1 that regulate the dynamics of lipolysis in human primary adipocytes. Cellular imaging combined with biochemical and biophysical analyses demonstrate that perilipin 1 specifically binds to cholesteryl esters, and that their dynamic properties direct segregation of perilipin 1 into topologically distinct micro domains on the lipid droplet. Together, our data points to a simple unifying mechanism that lipid assembly and segregation control lipolysis in human primary adipocytes.
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spelling oxford-uuid:4a45fd71-b213-4a30-bcea-b9d4a7b2fb9e2022-03-26T15:36:32ZVisualization of lipid directed dynamics of perilipin 1 in human primary adipocytesJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4a45fd71-b213-4a30-bcea-b9d4a7b2fb9eEnglishSymplectic Elements at OxfordSpringer Nature2017Hansen, JDe Maré, SJones, HGöransson, OLindkvist-Petersson, KPerilipin 1 is a lipid droplet coating protein known to regulate lipid metabolism in adipocytes by serving as a physical barrier as well as a recruitment site for lipases to the lipid droplet. Phosphorylation of perilipin 1 by protein kinase A rapidly initiates lipolysis, but the detailed mechanism on how perilipin 1 controls lipolysis is unknown. Here, we identify specific lipid binding properties of perilipin 1 that regulate the dynamics of lipolysis in human primary adipocytes. Cellular imaging combined with biochemical and biophysical analyses demonstrate that perilipin 1 specifically binds to cholesteryl esters, and that their dynamic properties direct segregation of perilipin 1 into topologically distinct micro domains on the lipid droplet. Together, our data points to a simple unifying mechanism that lipid assembly and segregation control lipolysis in human primary adipocytes.
spellingShingle Hansen, J
De Maré, S
Jones, H
Göransson, O
Lindkvist-Petersson, K
Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes
title Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes
title_full Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes
title_fullStr Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes
title_full_unstemmed Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes
title_short Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes
title_sort visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes
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