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Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
Author(s): Zacharias DA, Violin JD, Newton AC, Tsien RY
Source: SCIENCE    Volume: 296    Issue: 5569    Pages: 913-916    Published: MAY 3 2002  
Times Cited: 689     References: 22     
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.
Document Type: Article
Language: English
Reprint Address: Tsien, RY (reprint author), Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA
Addresses:
1. Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA
2. Univ Calif San Diego, Biomed Sci Grad Program, La Jolla, CA 92093 USA
3. Univ Calif San Diego, Howard Hughes Med Inst, La Jolla, CA 92093 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
Subject Category: Multidisciplinary Sciences
IDS Number: 549KF
ISSN: 0036-8075
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