Abstract:
:Coordination between sequential steps in synaptic vesicle endocytosis, including clathrin coat formation, fission, and uncoating, appears to involve proteinprotein interactions. Here, we show that compounds that disrupt interactions of the SH3 domain of endophilin with dynamin and synaptojanin impair synaptic vesicle endocytosis in a living synapse. Two distinct endocytic intermediates accumulated. Free clathrin-coated vesicles were induced by a peptide-blocking endophilin's SH3 domain and by antibodies to the proline-rich domain (PRD) of synaptojanin. Invaginated clathrin-coated pits were induced by the same peptide and by the SH3 domain of endophilin. We suggest that the SH3 domain of endophilin participates in both fission and uncoating and that it may be a key component of a molecular switch that couples the fission reaction to uncoating.
journal_name
Neuronjournal_title
Neuronauthors
Gad H,Ringstad N,Löw P,Kjaerulff O,Gustafsson J,Wenk M,Di Paolo G,Nemoto Y,Crun J,Ellisman MH,De Camilli P,Shupliakov O,Brodin Ldoi
10.1016/s0896-6273(00)00038-6subject
Has Abstractpub_date
2000-08-01 00:00:00pages
301-12issue
2eissn
0896-6273issn
1097-4199pii
S0896-6273(00)00038-6journal_volume
27pub_type
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