Protein Raft Trips

Abstract

Attention has been focused on lipid rafts--microdomains of the plasma membrane enriched in sphingolipid and cholesterol--in part because many proteins that take part in signaling across the plasma membrane are preferentially located in these structures. Zacharias et al. (see the Perspective by van Meer) studied targeting of proteins to lipid rafts by monitoring fluorescence resonance energy transfer (FRET) between mutants of cyan fluorescent protein (mCFP) and yellow fluorescent protein molecules (mYFP) that had been engineered to prevent the normal dimerization of these proteins (see the Perspective by Zacharias ). FRET was detected between a fusion protein of CFP with caveolin, which is known to localize to rafts, and YFP that was acylated on its amino terminus. Prenyl modification of YFP, however, did not target the protein to rafts. Thus, lipid modification of proteins can regulate localization, and hence the function, of various proteins in lipid rafts. D. A. Zacharias, J. D. Violin, A. C. Newton, R. Y. Tsien, Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296 , 913-916 (2002). [Abstract] [Full Text] G. van Meer, The different hues of lipid rafts. Science 296 , 855-857 (2002). [Abstract] [Full Text] D. A. Zacharias, Sticky caveats in an otherwise glowing report: Oligomerizing fluorescent proteins and their use in cell biology. Science's STKE (2002) http://www.stke.org/cgi/content/full/OC_sigtrans;2002/131/pe23 [Abstract] [Full Text]