Human stoned B interacts with AP-2 and synaptotagmin and facilitates clathrin-coated vesicle uncoating
AUTOR(ES)
Walther, Kristin
FONTE
Oxford University Press
RESUMO
Synaptic vesicle biogenesis involves the recycling of synaptic vesicle components by clathrin-mediated endocytosis from the presynaptic membrane. stoned B, 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 B (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 µ2 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1083948Documentos Relacionados
- Dual interaction of synaptotagmin with µ2- and α-adaptin facilitates clathrin-coated pit nucleation
- Evolving nature of the AP2 α-appendage hub during clathrin-coated vesicle endocytosis
- Uncoating of clathrin-coated vesicles by uncoating ATPase from developing peas.
- Association of the fusion protein NSF with clathrin-coated vesicle membranes.
- Interaction of CTLA-4 with AP50, a clathrin-coated pit adaptor protein
