Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin. / Gad, Helge; Ringstad, Niels; Löw, Peter; Kjaerulff, Ole; Gustafsson, Jenny; Wenk, Markus; Di Paolo, Gilbert; Nemoto, Yasuo; Crum, John; Ellisman, Mark H.; De Camilli, Pietro; Shupliakov, Oleg; Brodin, Lennart.
In: Neuron, Vol. 27, No. 2, 01.01.2000, p. 301-312.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin
AU - Gad, Helge
AU - Ringstad, Niels
AU - Löw, Peter
AU - Kjaerulff, Ole
AU - Gustafsson, Jenny
AU - Wenk, Markus
AU - Di Paolo, Gilbert
AU - Nemoto, Yasuo
AU - Crum, John
AU - Ellisman, Mark H.
AU - De Camilli, Pietro
AU - Shupliakov, Oleg
AU - Brodin, Lennart
PY - 2000/1/1
Y1 - 2000/1/1
N2 - 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 clathrincoated 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.
AB - 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 clathrincoated 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.
UR - http://www.scopus.com/inward/record.url?scp=0033678935&partnerID=8YFLogxK
U2 - 10.1016/S0896-6273(00)00038-6
DO - 10.1016/S0896-6273(00)00038-6
M3 - Article
C2 - 10985350
AN - SCOPUS:0033678935
VL - 27
SP - 301
EP - 312
JO - Neuron
JF - Neuron
SN - 0896-6273
IS - 2
ER -
ID: 40834662