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Journal of Lipid Research, Vol. 46, 1331-1338, June 2005
Copyright © 2005 by American Society for Biochemistry and Molecular Biology
PAT family proteins pervade lipid droplet cores
Institute for Arteriosclerosis Research, University of Münster, Münster, Germany
Published, JLR Papers in Press, March 1, 2005. DOI 10.1194/jlr.M400323-JLR200
1 To whom correspondence should be addressed. e-mail: robenek{at}uni-muenster.de
The PAT family proteins, named after perilipin, adipophilin, and the tail-interacting protein of 47 kDa (TIP47), are implicated in intracellular lipid metabolism. They associate with lipid droplets, but how is completely unclear. From immunofluorescence studies, they are reported to be restricted to the outer membrane monolayer enveloping the lipid droplet and not to enter the core. Recently, we found another kind of lipid droplet-associated protein, caveolin-1, inside lipid droplets. Using freeze-fracture immunocytochemistry and electron microscopy, we now describe the distributions of perilipin and caveolin-1 and of adipophilin and TIP47 in lipid droplets of adipocytes and macrophages. All of these lipid droplet-associated proteins pervade the lipid droplet core and hence are not restricted to the droplet surface. Moreover, lipid droplets are surprisingly heterogeneous with respect to their complements and their distribution of lipid droplet-associated proteins. Whereas caveolin-1 is synthesized in the endoplasmic reticulum and is transferred to the lipid droplet core by inundating lipids during droplet budding, the PAT proteins, which are synthesized on free ribosomes in the cytoplasm, evidently target to the lipid droplet after it has formed.
How the polar lipid droplet-associated proteins are accommodated among the essentially hydrophobic neutral lipids of the lipid droplet core remains to be determined.
Supplementary key words perilipin • adipophilin • tail-interacting protein of 47 kDa • freeze-fracture labeling
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