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

Hansen, Jesper S. LU ; De Maré, Sofia LU ; Jones, Helena A. LU ; Göransson, Olga LU and Lindkvist-Petersson, Karin LU (2017) In Scientific Reports 7(1).
Abstract

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... (More)

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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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Scientific Reports
volume
7
issue
1
publisher
Nature Publishing Group
external identifiers
  • scopus:85033391987
  • wos:000414644100004
ISSN
2045-2322
DOI
10.1038/s41598-017-15059-4
language
English
LU publication?
yes
id
b422b6b2-1087-4ffb-b7a5-8ece37dc4af3
date added to LUP
2017-11-20 08:28:42
date last changed
2018-01-16 13:25:51
@article{b422b6b2-1087-4ffb-b7a5-8ece37dc4af3,
  abstract     = {<p>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.</p>},
  articleno    = {15011},
  author       = {Hansen, Jesper S. and De Maré, Sofia and Jones, Helena A. and Göransson, Olga and Lindkvist-Petersson, Karin},
  issn         = {2045-2322},
  language     = {eng},
  month        = {11},
  number       = {1},
  publisher    = {Nature Publishing Group},
  series       = {Scientific Reports},
  title        = {Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes},
  url          = {http://dx.doi.org/10.1038/s41598-017-15059-4},
  volume       = {7},
  year         = {2017},
}