A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

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Citation Koh, T.W., Verstreken, P., Bellen, H.J. (2004). Dap160/Intersectin acts as a stabilizing scaffold required for synaptic development and vesicle endocytosis.  Neuron 43(2): 193--205. (Export to RIS)
FlyBase ID FBrf0179283
Publication Type Research paper
PubMed ID 15260956
PubMed Abstract We describe the isolation of mutations in dynamin-associated protein 160 kDa (dap160), the Drosophila homolog of intersectin, a putative adaptor for proteins involved in endocytosis, cytoskeletal regulation, and signaling. We show that partial loss-of-function mutants display temperature-sensitive (ts) paralysis, whereas null mutants show ts defects in endocytosis. Loss-of-function mutants exhibit bouton overgrowth at larval neuromuscular junctions (NMJs), but evoked neurotransmission is normal. Mutant NMJs show a mild endocytic defect at 22 degrees C, which is strongly enhanced at 34 degrees C. The levels of dynamin, synaptojanin and endophilin are severely reduced in dap160 mutant NMJs, suggesting that Dap160 serves to stabilize an endocytic macromolecular complex. Electron microscopy reveals fewer vesicles, aberrant large vesicles, and an accumulation of endocytic intermediates at active and periactive zones in mutant terminals. Our data suggest that Dap160, like dynamin, is involved in synaptic vesicle retrieval at active and periactive zones.
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Language of Publication English
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Publication Type Journal
Abbreviation Neuron
Title Neuron
Publication Year 1988-
ISBN/ISSN 0896-6273
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