Human stoned B interacts with AP-2 and synaptotagmin and facilitates clathrin-coated vesicle uncoating

Walther K., Krauss M., DİRİL M. K., Lemke S., Ricotta D., Honing S., ...More

EMBO REPORTS, vol.2, no.7, pp.634-640, 2001 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 2 Issue: 7
  • Publication Date: 2001
  • Doi Number: 10.1093/embo-reports/kve134
  • Journal Name: EMBO REPORTS
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.634-640
  • Dokuz Eylül University Affiliated: No


Synaptic vesicle biogenesis involves the recycling of synaptic vesicle components by clathrin-mediated endocytosis from the presynaptic membrane, stoned 8, a protein encoded by the stoned locus in Drosophila melanogaster has been shown to regulate vesicle recycling by interacting with synaptotagmin. We report here the identification and characterization of a human homolog of stoned 8 (hStnB). Human stoned B is a brain-specific protein which co-enriches with other endocytic proteins such as AP-2 in a crude synaptic vesicle fraction and at nerve terminals. A domain with homology to the medium chain of adaptor complexes binds directly to both AP-2 and synaptotagmin and competes with AP-2 for the same binding site within synaptotagmin. Finally we show that the mu2 homology domain of hStnB stimulates the uncoating of both clathrin and AP-2 adaptors from clathrin-coated vesicles. We hypothesize that hStnB regulates synaptic vesicle recycling by facilitating vesicle uncoating.