Cysteine-string proteins as templates for membrane fusion: models of synaptic vesicle exocytosis

Cysteine-string proteins are relatively small, cysteine-rich components of synaptic vesicle membranes. Recent investigations demonstrated that at least 11 of the 13 cysteine residues of the Torpedo cysteine-string protein are fatty acylated. This exceptional level of fatty acylation occurs along a s...

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Veröffentlicht in:Journal of theoretical biology 1995-02, Vol.172 (3), p.269-277
Hauptverfasser: Gundersen, Cameron B., Mastrogiacomo, Alessandro, Umbach, Joy A.
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container_title Journal of theoretical biology
container_volume 172
creator Gundersen, Cameron B.
Mastrogiacomo, Alessandro
Umbach, Joy A.
description Cysteine-string proteins are relatively small, cysteine-rich components of synaptic vesicle membranes. Recent investigations demonstrated that at least 11 of the 13 cysteine residues of the Torpedo cysteine-string protein are fatty acylated. This exceptional level of fatty acylation occurs along a short stretch (less than 25 residues) of amino acids which are flanked on either side by very polar amino and carboxy termini. This amphipathic structure may have unique capabilities to catalyze events at membrane interfaces. We propose two distinct pathways to explain how these capabilities might subserve membrane fusion and exocytosis.
doi_str_mv 10.1006/jtbi.1995.0023
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subjects Animals
Exocytosis - physiology
HSP40 Heat-Shock Proteins
Membrane Fusion
Membrane Proteins
Models, Biological
Nerve Tissue Proteins - metabolism
Synaptic Vesicles - physiology
title Cysteine-string proteins as templates for membrane fusion: models of synaptic vesicle exocytosis
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