期刊
FEBS LETTERS
卷 580, 期 23, 页码 5484-5491出版社
WILEY
DOI: 10.1016/j.febslet.2006.08.040
关键词
lipid droplet; PAT proteins; triacylglycerol; S3-12; TIP47; perilipin; ADRP; adipophilin; OXPAT; MLDP; PAT-1
资金
- NIDDK NIH HHS [DK059577, T32 DK07296, R01 DK068046, R01 DK54797] Funding Source: Medline
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. (c) 2006 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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