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Posttranslational membrane attachment and dynamic fatty acylation of a neuronal growth cone protein, GAP-43.
Abstract
Growth cones, the motile apparatus at the ends of elongating axons, are sites of extensive
and dynamic membrane-cytoskeletal interaction and insertion of new membrane into the
growing axon. One of the most abundant proteins in growth cone membranes is a protein
designated GAP-43, whose synthesis increases dramatically in most neurons during periods
of axon development or regeneration. We have begun to explore the role of GAP-43 in
growth cone membrane functions by asking how the protein interacts with those membranes.
Membrane-washing experiments indicate that mature GAP-43 is tightly bound to growth
cone membranes, and partitioning of Triton X-114-solubilized GAP-43 between detergent-enriched
and detergent-depleted phases indicates considerable hydrophobicity. The hydrophobic
behavior of the protein is modulated by divalent cations, particularly zinc and calcium.
In vivo labeling of GAP-43 in neonatal rat brain with [35S]methionine shows that GAP-43
is initially synthesized as a soluble protein that becomes attached to membranes posttranslationally.
In tissue culture, both rat cerebral cortex cells and neuron-like PC12 cells actively
incorporate [3H]palmitic acid into GAP-43. Isolated growth cones detached from their
cell bodies also incorporate labeled fatty acid into GAP-43, suggesting active turnover
of the fatty acid moieties on the mature protein. Hydrolysis of ester-like bonds with
neutral hydroxylamine removes the bound fatty acid and exposes new thiol groups on
GAP-43, suggesting that fatty acid is attached to the protein's only two cysteine
residues, located in a short hydrophobic domain at the amino terminus. Modulation
of the protein's hydrophobic behavior by divalent cations suggests that other domains,
containing large numbers of negatively charged residues, might also contribute to
GAP-43-membrane interactions. Our observations suggest a dynamic and reversible interaction
of GAP-43 with growth cone membranes.
Type
Journal articleSubject
BrainCerebral Cortex
Neurons
Axons
Cell Membrane
Animals
Rats, Inbred Strains
Rats
Cations, Divalent
Calcium
Zinc
Cysteine
Fatty Acids
Palmitic Acids
Palmitic Acid
Growth Substances
GAP-43 Protein
Membrane Proteins
Nerve Tissue Proteins
Phosphoproteins
Protein Processing, Post-Translational
Acylation
Solubility
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https://hdl.handle.net/10161/21965Published Version (Please cite this version)
10.1083/jcb.108.2.613Publication Info
Skene, JH; & Virág, I (1989). Posttranslational membrane attachment and dynamic fatty acylation of a neuronal growth
cone protein, GAP-43. The Journal of cell biology, 108(2). pp. 613-624. 10.1083/jcb.108.2.613. Retrieved from https://hdl.handle.net/10161/21965.This is constructed from limited available data and may be imprecise. To cite this
article, please review & use the official citation provided by the journal.
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Show full item recordScholars@Duke
Jesse Haynes Pate Skene
Associate Research Professor of Neurobiology
Extension of long axons is essential for the formation of connections in the developing
nervous system, and for effective regeneration of pathways interrupted by traumatic
injury, stroke, or other insults in the adult CNS. This laboratory is exploring
how changes in genes expression during development alter the ability of neurons to
support long axon extension, and the extent to which the re-activation of critical
genes limits regeneration in the adult CNS. Global gene expression p

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