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Partitioning of Lipid-Modified Monomeric GFPs into Membrane Microdomains of Live Cells
David A. Zacharias,13*Jonathan D. Violin,12*Alexandra C. Newton,1Roger Y. Tsien13
Many proteins associated with the plasma membrane are
known to partition into submicroscopic sphingolipid- and
cholesterol-richdomains called lipid rafts, but the determinants
dictating thissegregation of proteins in the membrane are poorly
understood.We suppressed the tendency of Aequorea
fluorescent proteins todimerize and targeted these variants to the
plasma membrane usingseveral different types of lipid anchors.
Fluorescence resonanceenergy transfer measurements in living cells
revealed that acylbut not prenyl modifications promote clustering in
lipid rafts.Thus the nature of the lipid anchor on a protein is
sufficientto 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.
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}ucsd.edu
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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.