Ontology highlight
ABSTRACT:
SUBMITTER: Winther AM
PROVIDER: S-EPMC4067270 | biostudies-literature | 2013 Feb
REPOSITORIES: biostudies-literature
Winther Åsa M E ÅM Jiao Wei W Vorontsova Olga O Rees Kathryn A KA Koh Tong-Wey TW Sopova Elena E Schulze Karen L KL Bellen Hugo J HJ Shupliakov Oleg O
Journal of cell science 20130115 Pt 4
Dynamin-associated protein 160 kDa (Dap160)/intersectin interacts with several synaptic proteins and affects endocytosis and synapse development. The functional role of the different protein interaction domains is not well understood. Here we show that Drosophila Dap160 lacking the dynamin-binding SH3 domains does not affect the development of the neuromuscular junction but plays a key role in synaptic vesicle recycling. dap160 mutants lacking dynamin-interacting domains no longer accumulate dyn ...[more]