Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin. / Gad, H; Ringstad, N; Löw, P; Kjaerulff, O; Gustafsson, J; Wenk, M; Di Paolo, G; Nemoto, Y; Crun, J; Ellisman, M H; De Camilli, P; Shupliakov, O; Brodin, L.

In: Neuron, Vol. 27, No. 2, 2000, p. 301-12.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

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, L 2000, 'Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin.', Neuron, vol. 27, no. 2, pp. 301-12.

APA

Gad, H., Ringstad, N., Löw, P., Kjaerulff, O., Gustafsson, J., Wenk, M., Di Paolo, G., Nemoto, Y., Crun, J., Ellisman, M. H., De Camilli, P., Shupliakov, O., & Brodin, L. (2000). Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin. Neuron, 27(2), 301-12.

Vancouver

Gad H, Ringstad N, Löw P, Kjaerulff O, Gustafsson J, Wenk M et al. Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin. Neuron. 2000;27(2):301-12.

Author

Gad, H ; Ringstad, N ; Löw, P ; Kjaerulff, O ; Gustafsson, J ; Wenk, M ; Di Paolo, G ; Nemoto, Y ; Crun, J ; Ellisman, M H ; De Camilli, P ; Shupliakov, O ; Brodin, L. / Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin. In: Neuron. 2000 ; Vol. 27, No. 2. pp. 301-12.

Bibtex

@article{8b4ac7c0752011dd8d9f000ea68e967b,
title = "Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin.",
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.",
author = "H Gad and N Ringstad and P L{\"o}w and O Kjaerulff and J Gustafsson and M Wenk and {Di Paolo}, G and Y Nemoto and J Crun and Ellisman, {M H} and {De Camilli}, P and O Shupliakov and L Brodin",
note = "Keywords: Adaptor Proteins, Signal Transducing; Animals; Binding, Competitive; Carrier Proteins; Clathrin; Cloning, Molecular; Coated Pits, Cell-Membrane; Dynamins; GTP Phosphohydrolases; Lampreys; Microinjections; Molecular Sequence Data; Nerve Tissue Proteins; Peptide Fragments; Phosphoric Monoester Hydrolases; Sequence Homology, Amino Acid; Synaptic Vesicles; src Homology Domains",
year = "2000",
language = "English",
volume = "27",
pages = "301--12",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "2",

}

RIS

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, H

AU - Ringstad, N

AU - Löw, P

AU - Kjaerulff, O

AU - Gustafsson, J

AU - Wenk, M

AU - Di Paolo, G

AU - Nemoto, Y

AU - Crun, J

AU - Ellisman, M H

AU - De Camilli, P

AU - Shupliakov, O

AU - Brodin, L

N1 - Keywords: Adaptor Proteins, Signal Transducing; Animals; Binding, Competitive; Carrier Proteins; Clathrin; Cloning, Molecular; Coated Pits, Cell-Membrane; Dynamins; GTP Phosphohydrolases; Lampreys; Microinjections; Molecular Sequence Data; Nerve Tissue Proteins; Peptide Fragments; Phosphoric Monoester Hydrolases; Sequence Homology, Amino Acid; Synaptic Vesicles; src Homology Domains

PY - 2000

Y1 - 2000

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 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.

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 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.

M3 - Journal article

C2 - 10985350

VL - 27

SP - 301

EP - 312

JO - Neuron

JF - Neuron

SN - 0896-6273

IS - 2

ER -

ID: 5750080