The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling

Anna Elisabetta Salcini, Massimo Antonio Hilliard, Assunta Croce, Salvatore Arbucci, Paola Luzzi, Carlo Tacchetti, Laurie Daniell, Pietro De Camilli, Pier Giuseppe Pelicci, Pier Paolo Di Fiore, Paolo Bazzicalupo

Research output: Contribution to journalArticlepeer-review


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 module1,2, and that are involved in many aspects of intracellular vesicular sorting3. Although biochemical and functional studies have implicated Eps15 in endocytosis4,5, 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 defect6, resulted in a worsening of the dyn-1 phenotype and uncoordination at the permissive temperature. Thus, ehs-1 and dyn-1 interact genetically. Moreover, mammalian Eps15 and dynamin protein were shown to interact in vivo. Taken together, our results indicate that EHS-1 acts in synaptic vesicle recycling and that its function might be linked to that of dynamin.

Original languageEnglish
Pages (from-to)755-760
Number of pages6
JournalNature Cell Biology
Issue number8
Publication statusPublished - 2001

ASJC Scopus subject areas

  • Cell Biology


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