The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Obese Yeast: Triglyceride Lipolysis Is Functionally Conserved from Mammals to Yeast
Open accessAbstract
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.
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Cites
Global analysis of protein localization in budding yeast
Huh, W.-K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., & O'Shea, E. K. (2003) · Nature · doi:10.1038/nature02026 · Cited by 4,248
A war on obesity, not the obese.
Friedman, J. M. (2003) · Science · doi:10.1126/science.1079856 · Cited by 375
Wong, H., & Schotz, M. C. (2002) · Journal of Lipid Research · doi:10.1194/jlr.r200007-jlr200 · Cited by 298
Cited by
Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores.
Zechner, R., Kienesberger, P. C., Haemmerle, G., Zimmermann, R., & Lass, A. (2009) · Journal of Lipid Research · doi:10.1194/jlr.r800031-jlr200 · Cited by 576
Self-citationMiller, R., Wu, G., Deshpande, R. R., Vieler, A., Gärtner, K., Li, X., Moellering, E. R., Zäuner, S., Cornish, A. J., Liu, B., et al. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.165159 · Cited by 511
Control of Lipid Accumulation in the Yeast Yarrowia lipolytica
Beopoulos, A., Mrozova, Z., Thevenieau, F., Le Dall, M.-T., Hapala, I., Papanikolaou, S., Chardot, T., & Nicaud, J.-M. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.01412-08 · Cited by 401
Li, X., Zhang, R., Patena, W., Gang, S. S., Blum, S. R., Ivanova, N., Yue, R., Robertson, J. M., Lefebvre, P. A., Fitz-Gibbon, S. T., et al. (2016) · The Plant Cell · doi:10.1105/tpc.15.00465 · Cited by 355
Yeast lipid metabolism at a glance
Klug, L., & Daum, G. (2014) · FEMS Yeast Research · doi:10.1111/1567-1364.12141 · Cited by 349
Metadata
- Authors
- Kurat, C. F., Natter, K., Petschnigg, J., Wolinski, H., Scheuringer, K., Scholz, H., Zimmermann, R., Leber, R., Zechner, R., & Kohlwein, S. D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-01
- Volume
- 281
- Issue
- 1
- Pages
- 491-500
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1980783399
- Cited by
- 322
- References
- 3
- FWCI
- 5.34
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kurat, C. F., Natter, K., Petschnigg, J., Wolinski, H., Scheuringer, K., Scholz, H., Zimmermann, R., Leber, R., Zechner, R., & Kohlwein, S. D. (2006). Obese Yeast: Triglyceride Lipolysis Is Functionally Conserved from Mammals to Yeast. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m508414200
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
