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- W2058644508 abstract "The mammalian protein Eps15 is phosphorylated by EGF receptor tyrosine kinase and has been shown to interact with several components of the endocytic machinery. We have identified a hypomorphic Eps15 mutant in Drosophila which shows reversible paralysis and an altered physiology at restrictive temperatures. In addition, the temperature-sensitive paralytic defect of shibire mutant is enhanced by this mutant. Eps15 is enriched in the larval neuromuscular junction in endocytic ‘hot spots’ in a pattern similar to Dynamin. Eps15 mutants show a decrease in the α-Adaptin levels at the larval neuromuscular junction synapse. Genetic and biochemical studies of interactions with components of the endocytic machinery suggest that Eps15 has an important role in synaptic vesicle recycling and regulates recruitment of α-Adaptin." @default.
- W2058644508 created "2016-06-24" @default.
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- W2058644508 date "2006-07-01" @default.
- W2058644508 modified "2023-09-30" @default.
- W2058644508 title "Drosophila homologue of Eps15 is essential for synaptic vesicle recycling" @default.
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- W2058644508 doi "https://doi.org/10.1016/j.yexcr.2006.03.030" @default.
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