High impact information on Eps-15

• Finally, we demonstrate that the isolated UIMs from both epsin and an unrelated monoubiquitinated protein, Eps15, are sufficient to promote ubiquitination of a chimeric glutathione-S-transferase (GST)-UIM fusion protein [1].
• 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 alpha-Adaptin [2].
• Eps15 is enriched in the larval neuromuscular junction in endocytic 'hot spots' in a pattern similar to Dynamin [2].
• Drosophila homologue of Eps15 is essential for synaptic vesicle recycling [2].
• Eps15 mutants show a decrease in the alpha-Adaptin levels at the larval neuromuscular junction synapse [2].

Associations of Eps-15 with chemical compounds

• The mammalian protein Eps15 is phosphorylated by EGF receptor tyrosine kinase and has been shown to interact with several components of the endocytic machinery [2].

Other interactions of Eps-15

• The STNB protein contains a domain that has homology with the mu-subunit of the AP (adaptor protein) complex, as well as a number of NPF (Asp-Pro-Phe) motifs known to bind EH (Eps15 homology) domains [3].
• Analyses of eps15 dap160 double mutants suggest that Eps15 functions in concert with Dap160 during SV endocytosis [4].

References