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Papers In Press, published online ahead of print February 1, 2010
J. Lipid Res., doi:10.1194/jlr.R003582

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Journal of Lipid Research, Vol. 51, 262-273, February 2010
Copyright © 2010 by American Society for Biochemistry and Molecular Biology

Thematic Review

Proteomic insights into an expanded cellular role for cytoplasmic lipid droplets^[S]

Brittany D. M. Hodges and Christine C. Wu¹

Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO

¹ To whom correspondence should be addressed. e-mail: christine.wu{at}ucdenver.edu

Cytoplasmic lipid droplets (CLDs) are cellular structures composed of a neutral lipid core surrounded by a phospholipid monolayer of amphipathic lipids and a variety of proteins. CLDs have classically been regarded as cellular energy storage structures. However, recent proteomic studies reveal that, although many of the proteins found to associate with CLDs are connected to lipid metabolism, storage, and homeostasis, there are also proteins with no obvious connection to the classical function and typically associated with other cellular compartments. Such proteins are termed refugee proteins, and their presence suggests that CLDs may serve an expanded role as a dynamic protein storage site, providing a novel mechanism for the regulation of protein function and transport.

Supplementary key words adipose differentiation related protein • adipophilin • PAT-family proteins • protein sequestration • mass spectrometry

Abbreviations: ADRP, adipose differentiation related protein or adipophilin; ARF, ADP ribosylation factor; CLD, cytoplasmic lipid droplet; CHO, Chinese hamster ovary; 1D, one dimensional; 2D, two dimensional; EM, electron microscopy; ER, endoplasmic reticulum; HCV, hepatitis C virus; MFG, milk fat globule; MFGM, milk fat globule membrane; PLD, phospholipase D

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