Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-11-19
pubmed:abstractText
We describe the isolation and characterization of Drosophila synaptojanin (synj) mutants. synj encodes a phosphatidylinositol phosphatase involved in clathrin-mediated endocytosis. We show that Synj is specifically localized to presynaptic terminals and is associated with synaptic vesicles. The electrophysiological and ultrastructural defects observed in synj mutants are strikingly similar to those found in endophilin mutants, and Synj and Endo colocalize and interact biochemically. Moreover, synj; endo double mutant synaptic terminals exhibit properties that are very similar to terminals of each single mutant, and overexpression of Endophilin can partially rescue the functional defects in partial loss-of-function synj mutants. Interestingly, Synj is mislocalized and destabilized at synapses devoid of Endophilin, suggesting that Endophilin recruits and stabilizes Synj on newly formed vesicles to promote vesicle uncoating. Our data also provide further evidence that kiss-and-run is able to maintain neurotransmitter release when synapses are not extensively challenged.
pubmed:grant
pubmed:commentsCorrections
pubmed:keyword
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
733-48
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:14622578-Adaptor Proteins, Signal Transducing, pubmed-meshheading:14622578-Animals, pubmed-meshheading:14622578-Animals, Genetically Modified, pubmed-meshheading:14622578-Carrier Proteins, pubmed-meshheading:14622578-Cell Differentiation, pubmed-meshheading:14622578-Clathrin, pubmed-meshheading:14622578-Down-Regulation, pubmed-meshheading:14622578-Drosophila melanogaster, pubmed-meshheading:14622578-Endocytosis, pubmed-meshheading:14622578-Female, pubmed-meshheading:14622578-Gene Expression Regulation, Developmental, pubmed-meshheading:14622578-Male, pubmed-meshheading:14622578-Membrane Fusion, pubmed-meshheading:14622578-Microscopy, Electron, pubmed-meshheading:14622578-Mutation, pubmed-meshheading:14622578-Nerve Tissue Proteins, pubmed-meshheading:14622578-Phenotype, pubmed-meshheading:14622578-Phosphoric Monoester Hydrolases, pubmed-meshheading:14622578-Photoreceptor Cells, Invertebrate, pubmed-meshheading:14622578-Presynaptic Terminals, pubmed-meshheading:14622578-Synaptic Transmission, pubmed-meshheading:14622578-Synaptic Vesicles
pubmed:year
2003
pubmed:articleTitle
Synaptojanin is recruited by endophilin to promote synaptic vesicle uncoating.
pubmed:affiliation
Department of Molecular and Human Genetics, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
pubmed:publicationType
Journal Article, Comment, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't