Charles J. Schultz

TL;DR: The properties, distribution, localization, and potential functions of perilipins and ADRP, as well as those of vimentin and the recently-described 'capsular' proteins, in lipid storage and metabolism are discussed.

TL;DR: It is shown that GFP-tagged TIP47 co-localizes with isolated intracellular lipid droplets and that related proteins from species as diverse as Drosophila and Dictyostelium can also target mammalian or Drosophile lipid droplet surfaces in vivo, strongly indicating that they have a common function for lipid deposition and/or mobilization.

TL;DR: The participation of perilipin A is indicated by the findings that this protein can protect neutral lipids within droplets from hydrolysis, but active participation in the lipolytic reaction is yet to be proved.

TL;DR: There is no evidence that perilipins participate directly in, or are necessary for, lipid catabolism, and the result is that neutral lipids are encased in perilipin-bounded droplets.

TL;DR: A role for ADrP is suggested in this novel mechanism for the transfer of lipid between lipofibroblasts and EPII cells, which is a precursor for surfactant phospholipid synthesis by alveolar type II epithelial (EPII) cells.