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Dynamic Activity of Lipid Droplets: Protein Phosphorylation and GTP-Mediated Protein Translocation
Abstract
Lipid droplet is a cellular organelle with a neutral lipid core surrounded by a phospholipid monolayer and coated with structural as well as functional proteins. The determination of these proteins, especially their functional regulations and dynamic movement on and off droplets, holds a key to resolving the biological functions of the cellular organelle. To address this, we carried out a comprehensive proteomic study that includes a complete proteomic, a phosphoprotein proteomic, and a comparative proteomic analysis using purified lipid droplets and mass spectrometry techniques. The complete proteome identified 125 proteins of which 70 proteins had not been identified on droplets of mammalian cells previously. In phosphoprotein proteomic analysis, 7 functional lipid droplet proteins were determined to be phosphorylated, including adipose differentiation related protein (ADRP/ADFP), two Rab proteins, and four lipid metabolism enzymes, including adipose triglyceride lipase (ATGL). To understand the dynamics of lipid droplets, GTP-dependent protein recruitment was analyzed by comparative proteomics. Arf1 and some of its coatomers, three other Arfs, several other small G-proteins including 3 Rabs, and several lipid synthetic enzymes were recruited from cytosol to purified droplets. Together, the present study suggests that lipid droplet is an active and dynamic cellular organelle that governs lipid homeostasis and intracellular trafficking through protein phosphorylation as well as GTP-regulated protein translocation.
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Molecular anatomy of a trafficking organelle
Takamori, S., Holt, M., Stenius, K., Lemke, E. A., Grønborg, M., Riedel, D., Urlaub, H., Schenck, S., Brügger, B., Ringler, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.10.030 · Cited by 2,373
A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic
Short, B., Preisinger, C., Körner, R., Kopajtich, R., Byron, O., & Barr, F. A. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200108079 · Cited by 226
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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
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Beller, M., Thiel, K., Thul, P. J., & Jäckle, H. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.03.022 · Cited by 263
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Dong, H., & Czaja, M. J. (2011) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2011.02.003 · Cited by 197
Lipid droplets and steroidogenic cells
Shen, W.-J., Azhar, S., & Kraemer, F. B. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.11.024 · Cited by 175
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Khan, S. A., Wollaston-Hayden, E. E., Markowski, T. W., Higgins, L., & Mashek, D. G. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m056812 · Cited by 64
Lipid droplets as signaling platforms linking metabolic and cellular functions
Arrese, E. L., Saudale, F. Z., & Soulages, J. L. (2014) · Lipid Insights · doi:10.4137/lpi.s11128 · Cited by 54
Ogasawara, J., Izawa, T., Sakurai, T., Sakurai, T., Shirato, K., Ishibashi, Y., Ishida, H., Ohno, H., & Kizaki, T. (2015) · Journal of Obesity · doi:10.1155/2015/473430 · Cited by 31
DFCP1 is a regulator of starvation-driven ATGL-mediated lipid droplet lipolysis
Ismail, V. A., Schuetz, M., Baker, Z. N., Castillo-Badillo, J. A., Naismith, T. V., Pagliarini, D. J., & Kast, D. J. (2025) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100700 · Cited by 5
Metadata
- Authors
- Bartz, R., Zehmer, J. K., Zhu, M., Chen, Y., Serrero, G., Zhao, Y., & Liu, P.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-07-03
- Volume
- 6
- Issue
- 8
- Pages
- 3256-3265
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2046333439
- Cited by
- 316
- References
- 2
- FWCI
- 9.38
- Type
- journal article
- Language
- en
- Open access
- closed
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