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

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          Abstract

          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 Aequorea fluorescent 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.

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          Author and article information

          Journal
          Science
          Science
          American Association for the Advancement of Science (AAAS)
          0036-8075
          1095-9203
          May 03 2002
          May 03 2002
          : 296
          : 5569
          : 913-916
          Affiliations
          [1 ]Department of Pharmacology,
          [2 ]Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093–0647, USA.
          [3 ]Biomedical Sciences Graduate Program, and
          Article
          10.1126/science.1068539
          11988576
          9b2fbc99-ca2b-4723-97aa-9f797133f23f
          © 2002
          History

          Quantitative & Systems biology,Biophysics
          Quantitative & Systems biology, Biophysics

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