Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-1-25
pubmed:abstractText
A brief review is presented of investigations of a novel family of synaptic vesicle proteins, the cysteine string proteins (csps). Studies of csp mutants in Drosophila reveal that csps are crucial components of the excitation-secretion machinery at nerve terminals. Current data cannot distinguish between a primary role of csps in modulating calcium ion influx at the nerve terminal versus a more-direct role in the exocytotic cascade. In this context, the remarkable post-translational modification of csps, namely the fatty acylation of as many as 12 of the 13 cysteine residues of the Torpedo protein, suggests that csps may participate more directly in the process of membrane fusion that underlies exocytosis. This would be achieved by using the fatty acyl chains of the csps as templates for 'lipid flow' that would allow the fusion of vesicular and plasma membranes. These hypotheses provide a useful framework for empirical tests of the role of csps in nerve terminal function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0928-4257
pubmed:author
pubmed:issnType
Print
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-101
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Cysteine string proteins and presynaptic function.
pubmed:affiliation
Department of Molecular and Medical Pharmacology, UCLA School of Medicine 90024, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review