Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2019 Feb 21;8(2):187. doi: 10.3390/cells8020187

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

LD schematic representation. LDs have a core composed of triacylglycerol (TAG) and cholesteryl ester (CE), surrounded by a phospholipid monolayer. Some proteins binding to the phospholipid monolayer are involved in neutral lipid metabolism. In the stimulated condition, ABHD5 binds to and activates ATGL, and TAG is hydrolyzed sequentially by ATGL, hormone-sensitive lipase (HSL), and monoacyl-glycerol lipase (MGL) to generate fatty acid (FA) and glycerol. In hepatic and muscle cells, pigment epithelium-derived factor (PEDF) stimulates lipolysis by binding ATGL. In the unstimulated state, lipolysis is inhibited by the association of ATGL with G0/G1 switch gene 2 (G0S2), hypoxia-inducible LD-associated protein (HILPDA), and cell death activator CIDE-3 (CIDEC) and by the interaction between ABHD5 and perilipin (PLIN) proteins. In addition, ATGL can interact with LC3, an autophagic protein. Direct ATGL–LC3 binding can facilitate correct ATGL localization on the LD surface.