Structure-function analysis of the cysteine string protein in Drosophila: cysteine string, linker and C terminus.
2004
SUMMARY Cysteine string proteins (CSPs) are conserved secretory vesicle proteins
involved in regulating neurotransmitter and peptide release. While the
function of the J-domain has been studied in detail, little is known about
other conserved regions. We have constructed mutant genes coding for proteins
with modified cysteine string, linker region or C terminus and transformed
them into Csp null-mutant Drosophila . In the living animal,
mutated CSP lacking all cysteines fails to associate with membranes, does not
concentrate in synaptic terminals, and cannot rescue adult
temperature-sensitive paralysis and short life span, both prominent null
mutant phenotypes. A mutant protein with 5 instead of 11 string cysteines
appears to be normally targeted but cannot rescue paralysis at 37°C. We
propose that the cysteine string, in addition to its role in targeting, may be
essential for a function of CSP that is dependent on the number of cysteines
in the string. A deletion in the linker region or the C terminus does not
affect CSP targeting, and function in adults is only marginally impaired.
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