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Vol. 12, Issue 11, 3601-3617, November 2001
and
§
When variably fatty acylated N-terminal amino acid sequences were
appended to a green fluorescent reporter protein (GFP), chimeric GFPs
were localized to different membranes in a fatty acylation-dependent
manner. To explore the mechanism of localization, the properties of
acceptor membranes and their interaction with acylated chimeric GFPs
were analyzed in COS-7 cells. Myristoylated GFPs containing a
palmitoylated or polybasic region colocalized with cholesterol and
ganglioside GM1, but not with caveolin, at the plasma
membrane and endosomes. A dipalmitoylated GFP chimera colocalized with
cholesterol and GM1 at the plasma membrane and with
caveolin in the Golgi region. Acylated GFP chimeras did not cofractionate with low-density caveolin-rich lipid rafts prepared with
Triton X-100 or detergent-free methods. All GFP chimeras, but not
full-length p62c-yes and caveolin, were readily solubilized
from membranes with various detergents. These data suggest that,
although N-terminal acylation can bring GFP to cholesterol and
sphingolipid-enriched membranes, protein-protein interactions are
required to localize a given protein to detergent-resistant membranes
or caveolin-rich membranes. In addition to restricting acceptor
membrane localization, N-terminal fatty acylation could represent an
efficient means to enrich the concentration of signaling proteins in
the vicinity of detergent-resistant membranes and facilitate
protein-protein interactions mediating transfer to a
detergent-resistant lipid raft core.
Department of Cell Biology and *M.D./Ph.D. Program,
Faculty of Medicine and Dentistry, University of Alberta, Edmonton,
Alberta, Canada T6G 2H7
Present address: Department of
Ophthalmology, University of Alberta, 2319 ATC, Royal Alexandra
Hospital, 10240 Kingsway Avenue, Edmonton, Alberta, Canada T5H 3V9.
§
Corresponding author. E-mail address:
Luc.Berthiaume{at}ualberta.ca.
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