
-   Protein Accession: Q96AD5
-   Size: 504 amino acids
-   Molecular mass: 55316 Da
-   Domains: Acyl_Trfase/lysoPLipase, PLPL, PNPLA2, PNPLA_dom
-   Family: Patatin like phospholipase domain containing Lipases [PMID: 19029121]
-   Adipose triglyceride lipase (ATGL) is the key-enzyme for the release of fatty acids (FAs) from triacylglycerol (TG) stores during intracellular lipolysis and produces FAs used for energy production [PMID: 28925902]. Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets [PMID: 15550674, PMID: 15364929, PMID: 16150821, PMID: 17603008, PMID: 16239926, PMID: 34903883]. Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone and acts coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade. Also possesses acylglycerol transacylase and phospholipase A2 activities [PMID: 15364929, PMID: 17032652, PMID: 17603008]. Transfers fatty acid from triglyceride to retinol, hydrolyzes retinylesters, and generates 1,3-diacylglycerol from triglycerides [PMID: 17603008]. Regulates adiposome size and may be involved in the degradation of adiposomes [PMID: 16239926]. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion. Catalyzes the formation of an ester bond between hydroxy fatty acids and fatty acids derived from triglycerides or diglycerides to generate fatty acid esters of hydroxy fatty acids (FAHFAs) in adipocytes [PMID: 35676490].
-   ATGL include an N-terminal amphipathic helix (Ile10-Gly24) potentially involved in TG binding, and a hydrophobic region (Pro315-Pro360), which is considered to be responsible for the localization to LDs [PMID: 18445677]. The C-terminal region of human adipose triglyceride lipase affects enzyme activity and lipid droplet binding [PMID: 18445597]. C-terminal truncated versions of human ATGL (Q289X, deletion of 215 residues) fail to localize to LDs, but surprisingly exhibit higher lipolytic activity in vitro, indicating that the C-terminus of ATGL possesses auto-regulatory function [PMID: 18445597].
-   The surface of lipid droplets (LDs) is decorated by five members of the perilipin (Plin) family, Plin1-Plin5, which form a barrier to prevent the access of ATGL to triacylglycerol stores of the LD [PMID: 27431369]. Plin1 is to sequester the co-activator protein comparative gene identification 58 (CGI-58) preventing its stimulating interaction with ATGL [PMID: 28925902]. Chaperone-mediated autophagy mediates the degradation of Plin2 and Plin3 and thus aids in access of ATGL to LDs [PMID: 25961502]. The direct regulation of ATGL activity on the protein level involves the interaction with its co-activator protein comparative gene identification 58 (CGI-58), also known as alpha/beta hydrolase domain containing protein 5 (ABHD5), and inhibitor protein G0/G1 switch gene 2 (G0S2) [PMID: 16679289, PMID: 20676045].
