Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 49, Pages 41446-41457Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.400416
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Funding
- grant GOLD: Genomics Of Lipid-associated Disorders, which is part of the Austrian Genome Project GEN-AU: Genome Research in Austria
- Austrian Ministry of Science and Research
- Austrian Research Promotion Agency
- Doktoratskolleg [W901-B05DK]
- Wittgenstein Award [Z136]
- Austrian Science Fund
- City of Graz
- Province of Styria
- [P21296]
- [F30 SFB LIPOTOX]
- Austrian Science Fund (FWF) [Z136] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [F 3002, W 901, Z 136] Funding Source: researchfish
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Adipose triglyceride lipase (ATGL) is rate-limiting for the initial step of triacylglycerol (TAG) hydrolysis, generating diacylglycerol (DAG) and fatty acids. DAG exists in three stereochemical isoforms. Here we show that ATGL exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone. The selectivity of ATGL broadens to the sn-1 position upon stimulation of the enzyme by its co-activator CGI-58. sn-1,3 DAG is the preferred substrate for the consecutive hydrolysis by hormone-sensitive lipase. Interestingly, diacylglycerol-O-acyltransferase 2, present at the endoplasmic reticulum and on lipid droplets, preferentially esterifies sn-1,3 DAG. This suggests that ATGL and diacylglycerol-O-acyltransferase 2 act coordinately in the hydrolysis/re-esterification cycle of TAGs on lipid droplets. Because ATGL preferentially generates sn-1,3 and sn-2,3, it suggests that TAG-derived DAG cannot directly enter phospholipid synthesis or activate protein kinase C without prior isomerization.
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