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...
Main Authors: | , , , , |
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Format: | Journal article |
Language: | English |
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Springer Nature
2017
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_version_ | 1826270893363429376 |
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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. |
first_indexed | 2024-03-06T21:48:00Z |
format | Journal article |
id | oxford-uuid:4a45fd71-b213-4a30-bcea-b9d4a7b2fb9e |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T21:48:00Z |
publishDate | 2017 |
publisher | Springer Nature |
record_format | dspace |
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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