Adipose triglyceride lipase (ATGL) is the key-enzyme for the release of fatty acids (FAs)
from triacylglycerol (TG) stores during intracellular lipolysis producing FAs used for energy production.
There is growing evidence that the products and intermediates from lipolytic breakdown during the FA
mobilization process also have fundamental regulatory functions affecting cell signaling, gene expression,
metabolism, cell growth, cell death, and lipotoxicity. Regulation of ATGL is therefore vital for
maintaining a defined balance between lipid storage and mobilization. This review addresses the regulation
of ATGL activity at the post-translational level with special emphasis on protein-mediated interaction
at the site of hydrolytic action, namely to the lipid droplet.
Keywords: Lipolysis, ATGL, adipose triglyceride lipase, PNPLA2, patatin-like phospholipase domain-containing protein 2,
G0S2, G0/G1 switch gene 2, CGI-58, comparative gene identification 58, ABHD5, α/β hydrolase domain containing protein 5,
perilipin, Plin, cell death activator CIDE-3, CIDEC, fat-specific protein 27, FSP27, hypoxia-inducible lipid dropleT-associated,
HILPDA, pigment epithelium derived factor, PEDF, serpin family F member 1, SERPINF1, oleoyl-CoA, Atglistatin.
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