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Vol. 10, Issue 11, 3771-3786, November 1999
*Graduate Program, Several membrane-associating signals, including covalently linked
fatty acids, are found in various combinations at the N termini of
signaling proteins. The function of these combinations was investigated
by appending fatty acylated N-terminal sequences to green fluorescent
protein (GFP). Myristoylated plus mono/dipalmitoylated GFP chimeras and
a GFP chimera containing a myristoylated plus a polybasic domain were
localized similarly to the plasma membrane and endosomal vesicles, but
not to the nucleus. Myristoylated, nonpalmitoylated mutant chimeric
GFPs were localized to intracellular membranes, including endosomes and
the endoplasmic reticulum, and were absent from the plasma membrane,
the Golgi, and the nucleus. Dually palmitoylated GFP was localized to
the plasma membrane and the Golgi region, but it was not detected in
endosomes. Nonacylated GFP chimeras, as well as GFP, showed cytosolic
and nuclear distribution. Our results demonstrate that myristoylation
is sufficient to exclude GFP from the nucleus and associate with
intracellular membranes, but plasma membrane localization requires a
second signal, namely palmitoylation or a polybasic domain. The
similarity in localization conferred by the various myristoylated and
palmitoylated/polybasic sequences suggests that biophysical properties
of acylated sequences and biological membranes are key determinants in
proper membrane selection. However, dual palmitoylation in the absence
of myristoylation conferred significant differences in localization,
suggesting that multiple palmitoylation sites and/or enzymes may exist.
Departments of Cell Biology and Biochemistry,
Corresponding author. E-mail address:
luc.berthiaume{at}ualberta.ca.
Molecular Biology of the Cell
Vol. 10, 3771-3786, November 1999
Copyright © 1999 by The American Society for Cell Biology
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