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Science 296 (5569): 913-916

Copyright © 2002 by the American Association for the Advancement of Science

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

David A. Zacharias,13*dagger Jonathan D. Violin,12* Alexandra C. Newton,1 Roger Y. Tsien13ddagger

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.

1 Department of Pharmacology,
2 Biomedical Sciences Graduate Program, and
3 Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093-0647, USA.
*   These authors contributed equally to this work.

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

ddagger    To whom correspondence should be addressed. E-mail: rtsien{at}ucsd.edu

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M. Ohtsuka, S. Ogiwara, H. Miura, A. Mizutani, T. Warita, M. Sato, K. Imai, K. Hozumi, T. Sato, M. Tanaka, et al. (2010)
Nucleic Acids Res. 38, e198
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Intrinsic Cytoskeleton-Dependent Clustering of Influenza Virus M2 Protein with Hemagglutinin Assessed by FLIM-FRET.
B. Thaa, A. Herrmann, and M. Veit (2010)
J. Virol. 84, 12445-12449
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O-Glycosylation Modulates Proprotein Convertase Activation of Angiopoietin-like Protein 3: POSSIBLE ROLE OF POLYPEPTIDE GalNAc-TRANSFERASE-2 IN REGULATION OF CONCENTRATIONS OF PLASMA LIPIDS.
K. T.- B. G. Schjoldager, M. B. Vester-Christensen, E. P. Bennett, S. B. Levery, T. Schwientek, W. Yin, O. Blixt, and H. Clausen (2010)
J. Biol. Chem. 285, 36293-36303
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Coordination of Fc receptor signaling regulates cellular commitment to phagocytosis.
Y. Zhang, A. D. Hoppe, and J. A. Swanson (2010)
PNAS 107, 19332-19337
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The Anti-inflammatory Drug Indomethacin Alters Nanoclustering in Synthetic and Cell Plasma Membranes.
Y. Zhou, S. J. Plowman, L. M. Lichtenberger, and J. F. Hancock (2010)
J. Biol. Chem. 285, 35188-35195
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Cooperation Between the Septins and the Actomyosin Ring and Role of a Cell-Integrity Pathway During Cell Division in Fission Yeast.
J.-Q. Wu, Y. Ye, N. Wang, T. D. Pollard, and J. R. Pringle (2010)
Genetics 186, 897-915
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Farnesylated Nuclear Proteins Kugelkern and Lamin Dm0 Affect Nuclear Morphology by Directly Interacting with the Nuclear Membrane.
M. Polychronidou, A. Hellwig, and J. Grosshans (2010)
Mol. Biol. Cell 21, 3409-3420
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Regulation of Ras Localization by Acylation Enables a Mode of Intracellular Signal Propagation.
A. Lorentzen, A. Kinkhabwala, O. Rocks, N. Vartak, and P. I. H. Bastiaens (2010)
Science Signaling 3, ra68
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Lipid microdomains and the regulation of ion channel function.
C. Dart (2010)
J. Physiol. 588, 3169-3178
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Alternative Splicing of Neuroligin Regulates the Rate of Presynaptic Differentiation.
H. Lee, C. Dean, and E. Isacoff (2010)
J. Neurosci. 30, 11435-11446
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Quantitative Analysis of the Mechanism of Endocytic Actin Patch Assembly and Disassembly in Fission Yeast.
V. Sirotkin, J. Berro, K. Macmillan, L. Zhao, and T. D. Pollard (2010)
Mol. Biol. Cell 21, 2894-2904
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Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure.
N. I. Popescu, C. Lupu, and F. Lupu (2010)
Blood 116, 993-1001
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Polyglutamine Diseases: Where does Toxicity Come from? What is Toxicity? Where are We Going?.
T. Takahashi, S. Katada, and O. Onodera (2010)
J Mol Cell Biol 2, 180-191
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T-Cell Receptor Microclusters Critical for T-Cell Activation Are Formed Independently of Lipid Raft Clustering.
A. Hashimoto-Tane, T. Yokosuka, C. Ishihara, M. Sakuma, W. Kobayashi, and T. Saito (2010)
Mol. Cell. Biol. 30, 3421-3429
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Fluorescent Proteins and Their Applications in Imaging Living Cells and Tissues.
D. M. Chudakov, M. V. Matz, S. Lukyanov, and K. A. Lukyanov (2010)
Physiol Rev 90, 1103-1163
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