The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling. (Articolo in rivista) (literal)

Anno

• 2001-01-01T00:00:00+01:00 (literal)

Alternative label

• Salcini AE, Hilliard MA, Croce A, Arbucci S, Luzzi P, Tacchetti C, Daniell L, DeCamilli P, Pelicci PG, Di Fiore PP, Bazzicalupo P (2001)
  The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling.
  in Nature cell biology
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Salcini AE, Hilliard MA, Croce A, Arbucci S, Luzzi P, Tacchetti C, Daniell L, DeCamilli P, Pelicci PG, Di Fiore PP, Bazzicalupo P (literal)

Pagina inizio

• 755 (literal)

Pagina fine

• 760 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 3 (literal)

Rivista

• Nature cell biology (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling. (literal)

Abstract

• 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, and that are involved in many aspects of intracellular vesicular sorting. Although biochemical and functional studies have implicated Eps15 in endocytosis, 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 defect, 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. (literal)

Prodotto di

• Sviluppo e funzionamento dei sistemi complessi - Uso di modelli biologici (SV.P16.005.001) (Modulo)
• Institute of genetics and biophysics \"Adriano Buzzati Traverso\" (IGB) (Istituto)

Autore CNR

• PAOLO BAZZICALUPO (Unità di personale interno)

Incoming links:

Prodotto

• Institute of genetics and biophysics \"Adriano Buzzati Traverso\" (IGB) (Istituto)
• Sviluppo e funzionamento dei sistemi complessi - Uso di modelli biologici (SV.P16.005.001) (Modulo)

Autore CNR di

• PAOLO BAZZICALUPO (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Nature cell biology (Rivista)