Cysteine-string protein: the chaperone at the synapse.

摘要: Abstract: Cysteine-string protein (Csp) is a major synaptic vesicle and secretory granule first discovered in Drosophila Torpedo. Csps were subsequently identified from Xenopus, Caenorhabditis elegans, mammalian species. It clear the study of null mutant that Csp required for viability organism it has key role neurotransmitter release. In addition, other studies have directly implicated regulated exocytosis neuroendocrine endocrine cell types, its distribution suggests general exocytosis. An early hypothesis was functioned control voltage-gated Ca2+ channels. Csp, however, must an additional function as direct regulator exocytotic machinery changes expression modify extent triggered by permeabilised cells. possess cysteine-string domain highly palmitoylated confers membrane targeting. conserved “J” mediates binding to activation Hsp70/Hsc70 chaperone ATPases. This evidence implicate molecular chaperones synapse are likely correct conformational folding one or more components vesicular machinery. Targets include VAMP/synaptobrevin plasma syntaxin 1, significance which discussed possible models account current knowledge function.