The BioGRID | PUBLICATION VIEW

	EMBO Rep. Jul (2001); 2(7):634-40
Human stoned B interacts with AP-2 and synaptotagmin and facilitates clathrin-coated vesicle uncoating.
Walther K, Krauss M, Diril MK, Lemke S, Ricotta D, Honing S, Kaiser S, Haucke V
Zentrum Biochemie und Molekulare Zellbiologie, University of Gottingen, Humboldtallee 23, D-37073 Gottingen, Germany.
Abstract: 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 mu 2 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.
[PUBMED: 11454741]