Obese Yeast: Triglyceride Lipolysis Is Functionally Conserved from Mammals to Yeast

Storage and degradation of triglycerides are essential processes to ensure energy homeostasis and availability of precursors for membrane lipid synthesis. Recent evidence suggests that an emerging class of enzymes containing a conserved patatin domain are centrally important players in lipid degrada...

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Bibliographic Details
Published in:The Journal of biological chemistry 2006-01, Vol.281 (1), p.491-500
Main Authors: Kurat, Christoph F., Natter, Klaus, Petschnigg, Julia, Wolinski, Heimo, Scheuringer, Kim, Scholz, Harald, Zimmermann, Robert, Leber, Regina, Zechner, Rudolf, Kohlwein, Sepp D.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Conserved Sequence
Diglycerides - metabolism
Evolution, Molecular
Kinetics
Lipase - chemistry
Lipase - genetics
Lipase - metabolism
Lipolysis - physiology
Mammals
Mice
Molecular Sequence Data
Mutation
Obesity - enzymology
Protein Structure, Tertiary
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Substrate Specificity
Triglycerides - metabolism
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Summary:Storage and degradation of triglycerides are essential processes to ensure energy homeostasis and availability of precursors for membrane lipid synthesis. Recent evidence suggests that an emerging class of enzymes containing a conserved patatin domain are centrally important players in lipid degradation. Here we describe the identification and characterization of a major triglyceride lipase of the adipose triglyceride lipase/Brummer family, Tgl4, in the yeast Saccharomyces cerevisiae. Elimination of Tgl4 in a tgl3 background led to fat yeast, rendering growing cells unable to degrade triglycerides. Tgl4 and Tgl3 lipases localized to lipid droplets, independent of each other. Serine 315 in the GXSXG lipase active site consensus sequence of the patatin domain of Tgl4 is essential for catalytic activity. Mouse adipose triglyceride lipase (which also contains a patatin domain but is otherwise highly divergent in primary structure from any yeast protein) localized to lipid droplets when expressed in yeast, and significantly restored triglyceride breakdown in tgl4 mutants in vivo. Our data identify yeast Tgl4 as a functional ortholog of mammalian adipose triglyceride lipase.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M508414200