Premium
A proposed model of fat packaging by exchangeable lipid droplet proteins
Author(s) -
Wolins Nathan E.,
Brasaemle Dawn L.,
Bickel Perry E.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.040
Subject(s) - perilipin , lipid droplet , lipolysis , microbiology and biotechnology , chemistry , adipose tissue , cytosol , biochemistry , food science , biology , enzyme
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.