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Eps15 represents the prototype of a family of evolutionarily conserved proteins that are characterized by the presence of the EH domain, a protein–protein interaction module 1, 2, and that are involved in many aspects of intracellular vesicular sorting 3. Although biochemical and functional studies have implicated Eps15 in endocytosis 4, 5, its function in the endocytic machinery remains unclear. Here we show that the Caenorhabditis elegans gene, zk1248. 3 (ehs-1), is the orthologue of Eps15 in nematodes, and that its product, EHS-1, localizes to synaptic-rich regions. ehs-1-impaired worms showed temperature-dependent depletion of synaptic vesicles and uncoordinated movement. These phenotypes could be correlated with a presynaptic defect in neurotransmission. Impairment of EHS-1 function in dyn-1 (ky51) worms, which express a mutant form of dynamin and display a temperature-sensitive locomotion …