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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Synaptotagmin I is a high affinity receptor for clathrin AP-2: implications for membrane recycling.

In nerve terminals, Ca(2+)-stimulated synaptic vesicle exocytosis is rapidly followed by endocytosis. Synaptic vesicle endocytosis requires clathrin-coated pits similar to receptor-mediated endocytosis in fibroblasts. Binding of clathrin AP-2 (adaptor complex) to an unidentified high affinity membrane receptor appears to be necessary for coated pit assembly in fibroblasts. We now show that synaptic vesicles have a high affinity AP-2 site (KD, approximately 1 x 10(-10) M) similar to the one observed in fibroblasts. Using a combination of competition and direct binding assays, we demonstrate that synaptotagmin I, an intrinsic membrane protein of synaptic vesicles, has all of the properties of the AP-2 receptor and that AP-2 binds to the second C2 domain in the molecule. Thus, synaptotagmin I may be a multifunctional protein with a function in endocytosis in addition to the previously proposed role in exocytosis.[1]


  1. Synaptotagmin I is a high affinity receptor for clathrin AP-2: implications for membrane recycling. Zhang, J.Z., Davletov, B.A., Südhof, T.C., Anderson, R.G. Cell (1994) [Pubmed]
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