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.
(Less)
- author
- Hansen, Jesper S.
LU
; De Maré, Sofia
LU
; Jones, Helena A.
LU
; Göransson, Olga
LU
and Lindkvist-Petersson, Karin
LU
- organization
- publishing date
- 2017-11-08
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Scientific Reports
- volume
- 7
- issue
- 1
- article number
- 15011
- publisher
- Nature Publishing Group
- external identifiers
-
- scopus:85033391987
- pmid:29118433
- 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
- 2024-06-11 06:21:19
@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>}},
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}},
doi = {{10.1038/s41598-017-15059-4}},
volume = {{7}},
year = {{2017}},
}