A proposed model of fat packaging by exchangeable lipid droplet proteins

Nathan E. Wolins, Dawn L. Brasaemle, Perry E. Bickel

Research output: Contribution to journalShort surveypeer-review

320 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)5484-5491
Number of pages8
JournalFEBS Letters
Issue number23
StatePublished - Oct 9 2006


  • ADRP
  • Adipophilin
  • Lipid droplet
  • MLDP
  • PAT proteins
  • PAT-1
  • Perilipin
  • S3-12
  • TIP47
  • Triacylglycerol

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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