Partitioning of Lipid-Modified Monomeric GFPs into Membrane Microdomains of Live Cells

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Science  03 May 2002:
Vol. 296, Issue 5569, pp. 913-916
DOI: 10.1126/science.1068539

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Many proteins associated with the plasma membrane are known to partition into submicroscopic sphingolipid- and cholesterol-rich domains called lipid rafts, but the determinants dictating this segregation of proteins in the membrane are poorly understood. We suppressed the tendency of Aequoreafluorescent proteins to dimerize and targeted these variants to the plasma membrane using several different types of lipid anchors. Fluorescence resonance energy transfer measurements in living cells revealed that acyl but not prenyl modifications promote clustering in lipid rafts. Thus the nature of the lipid anchor on a protein is sufficient to determine submicroscopic localization within the plasma membrane.

  • * These authors contributed equally to this work.

  • Present address: Merck Research Laboratories, 3535 General Atomics Court, MRLSDB1, San Diego, CA 92121, USA.

  • To whom correspondence should be addressed. E-mail: rtsien{at}

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