The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Perilipin Controls Lipolysis by Regulating the Interactions of AB-hydrolase Containing 5 (Abhd5) and Adipose Triglyceride Lipase (Atgl)
Open accessAbstract
The mobilization of stored lipid by hormones is a fundamental function of fat cells, and there is strong evidence that perilipin (Plin), a lipid droplet scaffold, and adipose tissue triglyceride lipase (Atgl), a triglyceride-specific lipase, play critical roles. Previous work suggested that Abhd5, a protein activator of Atgl, coordinates with Plin in controlling basal and stimulated lipolysis; however, the underlying mechanism is controversial. The present experiments investigated protein trafficking and interactions among Plin, Atgl, and Abhd5 in live cells. The results demonstrate that Plin binds Abhd5 with high affinity and thereby suppresses the interaction of Abhd5 with Atgl. Sequestration of Abhd5 appears to a major mechanism by which Plin reduces basal lipolysis. Phosphorylation of Plin on serine 492 or serine 517 rapidly releases Abhd5 from Plin, allowing Abhd5 to directly interact with Atgl. Imaging experiments demonstrated that the Plin-dependent interaction of Abhd5 and Atgl occurs mainly, but not exclusively, on lipid droplets that contain Plin.
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Fat Mobilization in Adipose Tissue Is Promoted by Adipose Triglyceride Lipase
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Perilipin A Increases Triacylglycerol Storage by Decreasing the Rate of Triacylglycerol Hydrolysis
Brasaemle, D. L., Rubin, B., Harten, I. A., Gruia-Gray, J., Kimmel, A. R., & Londos, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007322200 · Cited by 438
A highly sensitive protein-protein interaction assay based on Gaussia luciferase
Remy, I., & Michnick, S. W. (2006) · Nature Methods · doi:10.1038/nmeth979 · Cited by 436
ATGL has a key role in lipid droplet/adiposome degradation in mammalian cells
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Cited by
Mechanisms of Insulin Action and Insulin Resistance
Petersen, M. C., & Shulman, G. I. (2018) · Physiological Reviews · doi:10.1152/physrev.00063.2017 · Cited by 3,028
What we talk about when we talk about fat
Rosen, E. D., & Spiegelman, B. M. (2014) · Cell · doi:10.1016/j.cell.2013.12.012 · Cited by 2,373
Inflammation and Lipid Signaling in the Etiology of Insulin Resistance
Glass, C. K., & Olefsky, J. M. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.001 · Cited by 935
Lipolysis – A highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores
Lass, A., Zimmermann, R., Oberer, M., & Zechner, R. (2011) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.10.004 · Cited by 640
Lipid droplet biogenesis and functions in health and disease
Zadoorian, A., Du, X., & Yang, H. (2023) · Nature Reviews Endocrinology · doi:10.1038/s41574-023-00845-0 · Cited by 617
Metadata
- Authors
- Granneman, J. G., Moore, H.-P. H., Krishnamoorthy, R., & Rathod, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-12
- Volume
- 284
- Issue
- 50
- Pages
- 34538-34544
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2014154105
- Cited by
- 386
- References
- 27
- FWCI
- 8.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Granneman, J. G., Moore, H.-P. H., Krishnamoorthy, R., & Rathod, M. (2009). Perilipin Controls Lipolysis by Regulating the Interactions of AB-hydrolase Containing 5 (Abhd5) and Adipose Triglyceride Lipase (Atgl). Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m109.068478
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