A proposed model of fat packaging by exchangeable lipid droplet proteins |
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Authors: | Wolins Nathan E Brasaemle Dawn L Bickel Perry E |
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Affiliation: | Department of Medicine, Division of Endocrinology, Metabolism and Lipid Research, Washington University School of Medicine, Saint Louis, MO 63110, USA. |
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Abstract: | Humans have evolved mechanisms of efficient fat storage to survive famine, but these mechanisms contribute to obesity in our current environment of plentiful food and reduced activity. Little is known about how animals package fat within cells. Five related structural proteins serve roles in packaging fat into lipid droplets. The proteins TIP47, S3-12, and OXPAT/MLDP/PAT-1 move from the cytosol to coat nascent lipid droplets during rapid fat storage. In contrast, perilipin and adipophilin constitutively associate with lipid droplets and play roles in sustained fat storage and regulation of lipolysis. Different tissues express different complements of these lipid droplet proteins. Thus, the tissue-specific complement of these proteins determines how tissues manage lipid stores. |
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Keywords: | Lipid droplet PAT proteins Triacylglycerol S3-12 TIP47 Perilipin ADRP Adipophilin OXPAT MLDP PAT-1 |
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