Perilipins, ADRP, and other proteins that associate with intracellular neutral lipid droplets in animal cells

Semin Cell Dev Biol. 1999 Feb;10(1):51-8. doi: 10.1006/scdb.1998.0275.


Although all animal cells package and store neutral lipids in discrete intracellular storage droplets, there is little information on the molecular processes that govern either the deposition or catabolism of the stored lipid components. Studies on adipocytes have uncovered the perilipins and ADRP, related proteins that appear to be intrinsic to the surfaces of intracellular lipid storage droplets. We discuss the properties, distribution, localization, and potential functions of these proteins, as well as those of vimentin and the recently-described 'capsular' proteins, in lipid storage and metabolism.

Publication types

  • Review

MeSH terms

  • 3T3 Cells
  • Animals
  • Carrier Proteins*
  • DNA-Binding Proteins*
  • Gene Expression Regulation / physiology
  • Intracellular Fluid / metabolism*
  • Intracellular Signaling Peptides and Proteins*
  • Lipid Metabolism*
  • Lipolysis / physiology
  • Membrane Proteins / metabolism*
  • Mice
  • Perilipin-1
  • Perilipin-2
  • Perilipin-3
  • Phosphoproteins / metabolism*
  • Pregnancy Proteins / physiology
  • RNA, Messenger / metabolism
  • Vesicular Transport Proteins
  • Vimentin / physiology


  • Carrier Proteins
  • DNA-Binding Proteins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • PLIN2 protein, human
  • PLIN3 protein, human
  • Perilipin-1
  • Perilipin-2
  • Perilipin-3
  • Phosphoproteins
  • Plin2 protein, mouse
  • Pregnancy Proteins
  • RNA, Messenger
  • Vesicular Transport Proteins
  • Vimentin