Posttranslational membrane attachment and dynamic fatty acylation of a neuronal growth cone protein, GAP-43.

dc.contributor.author

Skene, JH

dc.contributor.author

Virág, I

dc.date.accessioned

2021-01-02T07:00:51Z

dc.date.available

2021-01-02T07:00:51Z

dc.date.issued

1989-02

dc.date.updated

2021-01-02T07:00:49Z

dc.description.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.

dc.identifier.issn

0021-9525

dc.identifier.issn

1540-8140

dc.identifier.uri

https://hdl.handle.net/10161/21965

dc.language

eng

dc.publisher

Rockefeller University Press

dc.relation.ispartof

The Journal of cell biology

dc.relation.isversionof

10.1083/jcb.108.2.613

dc.subject

Brain

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Cerebral Cortex

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Neurons

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Axons

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Cell Membrane

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Animals

dc.subject

Rats, Inbred Strains

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Rats

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Cations, Divalent

dc.subject

Calcium

dc.subject

Zinc

dc.subject

Cysteine

dc.subject

Fatty Acids

dc.subject

Palmitic Acids

dc.subject

Palmitic Acid

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Growth Substances

dc.subject

GAP-43 Protein

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Membrane Proteins

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Nerve Tissue Proteins

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Phosphoproteins

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Protein Processing, Post-Translational

dc.subject

Acylation

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Solubility

dc.title

Posttranslational membrane attachment and dynamic fatty acylation of a neuronal growth cone protein, GAP-43.

dc.type

Journal article

duke.contributor.orcid

Skene, JH|0000-0003-3205-0697

pubs.begin-page

613

pubs.end-page

624

pubs.issue

2

pubs.organisational-group

School of Medicine

pubs.organisational-group

Neurobiology

pubs.organisational-group

Duke Science & Society

pubs.organisational-group

Duke Institute for Brain Sciences

pubs.organisational-group

Duke

pubs.organisational-group

Basic Science Departments

pubs.organisational-group

Initiatives

pubs.organisational-group

Institutes and Provost's Academic Units

pubs.organisational-group

University Institutes and Centers

pubs.publication-status

Published

pubs.volume

108

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