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J Biol Chem, Vol. 273, Issue 43, 28478-28485, October 23, 1998
From the Department of Biochemistry and Cell Biology, State
University of New York, Stony Brook, New York 11794-5215
GAP-43 is an abundant protein in axonal
growth cones of developing and regenerating neurons. We found that
GAP-43 was enriched in detergent-resistant membranes (DRMs) isolated by
Triton X-100 extraction from PC12 pheochromocytoma cells and could be
detected in detergent-insoluble plasma membrane remnants after
extraction of cells in situ. GAP-43 is palmitoylated at
Cys-3 and Cys-4. Mutation of either Cys residue prevented association
with DRMs. A hybrid protein containing the first 20 amino acid residues
of GAP-43 fused to
Association of GAP-43 with Detergent-resistant Membranes Requires
Two Palmitoylated Cysteine Residues
-galactosidase was targeted to DRMs even more efficiently than GAP-43 itself. We conclude that tandem palmitoylated Cys residues can target GAP-43 to DRMs, defining a new signal for DRM
targeting. We propose that tandem or closely spaced saturated fatty
acyl chains partition into domains or "rafts" in the liquid-ordered phase, or a phase with similar properties, in cell membranes. These
rafts are isolated as DRMs after detergent extraction. The brain-specific heterotrimeric G protein Go, which may be
regulated by GAP-43 in vitro, was also enriched in DRMs
from PC12 cells. Targeting of GAP-43 to rafts may function to
facilitate signaling through Go. In addition, raft
association may aid in sorting of GAP-43 into axonally directed
vesicles in the trans-Golgi network.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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