Premium
Human stoned B interacts with AP‐2 and synaptotagmin and facilitates clathrin‐coated vesicle uncoating
Author(s) -
Walther Kristin,
Krauss Michael,
Diril M Kasim,
Lemke Steffen,
Ricotta Doris,
Höning Stefan,
Kaiser Stephen,
Haucke Volker
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve134
Subject(s) - synaptotagmin 1 , clathrin , vesicle , microbiology and biotechnology , chemistry , biophysics , synaptic vesicle , biology , biochemistry , membrane
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.