La Trobe
1178223_Ma,X_2021.pdf (4.48 MB)

Validating an artificial organelle: Studies of lipid droplet-specific proteins on adiposome platform

Download (4.48 MB)
journal contribution
posted on 06.09.2021, 05:31 by X Ma, Zelun ZhiZelun Zhi, S Zhang, C Zhou, Adam MechlerAdam Mechler, P Liu
New strategies are urgently needed to characterize the functions of the lipid droplet (LD). Here, adiposome, an artificial LD mimetic platform, was validated by comparative in vitro bioassays. Scatchard analysis found that the binding of perilipin 2 (PLIN2) to the adiposome surface was saturable. Phosphatidylinositol (PtdIns) was found to inhibit PLIN2 binding while it did not impede perilipin 3 (PLIN3). Structural analysis combined with mutagenesis revealed that the 73rd glutamic acid of PLIN2 is significant for the effect of PtdIns on the PLIN2 binding. Furthermore, adiposome was also found to be an ideal platform for in situ enzymatic activity measurement of adipose triglyceride lipase (ATGL). The significant serine mutants of ATGL were found to cause the loss of lipase activity. Our study demonstrates the adiposome as a powerful, manipulatable model system that mimics the function of LD for binding and enzymatic activity studies of LD proteins in vitro.

History

Publication Date

20/08/2021

Journal

iScience

Volume

24

Issue

8

Article Number

102834

Pagination

25p.

Publisher

Elsevier

ISSN

2589-0042

Rights Statement

© 2021 The Authors. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Usage metrics

Categories

Exports