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Endophilin/sh3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis. / Ringstad, Niels; Gad, Helge; Löw, Peter; Di Paolo, Gilbert; Brodin, Lennart; Shupliakov, Oleg; De Camilli, Pietro.

в: Neuron, Том 24, № 1, 01.01.1999, стр. 143-154.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Ringstad, N, Gad, H, Löw, P, Di Paolo, G, Brodin, L, Shupliakov, O & De Camilli, P 1999, 'Endophilin/sh3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis', Neuron, Том. 24, № 1, стр. 143-154. https://doi.org/10.1016/S0896-6273(00)80828-4

APA

Ringstad, N., Gad, H., Löw, P., Di Paolo, G., Brodin, L., Shupliakov, O., & De Camilli, P. (1999). Endophilin/sh3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis. Neuron, 24(1), 143-154. https://doi.org/10.1016/S0896-6273(00)80828-4

Vancouver

Ringstad N, Gad H, Löw P, Di Paolo G, Brodin L, Shupliakov O и пр. Endophilin/sh3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis. Neuron. 1999 Янв. 1;24(1):143-154. https://doi.org/10.1016/S0896-6273(00)80828-4

Author

Ringstad, Niels ; Gad, Helge ; Löw, Peter ; Di Paolo, Gilbert ; Brodin, Lennart ; Shupliakov, Oleg ; De Camilli, Pietro. / Endophilin/sh3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis. в: Neuron. 1999 ; Том 24, № 1. стр. 143-154.

BibTeX

@article{e4b6071ca4704c5f8a12e2d46d9c1726,
title = "Endophilin/sh3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis",
abstract = "Endophilin/SH3p4 is a protein highly enriched in nerve terminals that binds the GTPase dynamin and the polyphosphoinositide phosphatase synaptojanin, two proteins implicated in synaptic vesicle endocytosis. We show here that antibody-mediated disruption of endophilin function in a tonically stimulated synapse leads to a block in the invagination of clathrin-coated pits adjacent to the active zone and therefore to a block of synaptic vesicle recycling. We also show that in a cell-free system, endophilin is not associated with clathrin coats and is a functional partner of dynamin. Our findings suggest that endophilin is part of a biochemical machinery that acts in trans to the clathrin coat from early stages to vesicle fission.",
author = "Niels Ringstad and Helge Gad and Peter L{\"o}w and {Di Paolo}, Gilbert and Lennart Brodin and Oleg Shupliakov and {De Camilli}, Pietro",
year = "1999",
month = jan,
day = "1",
doi = "10.1016/S0896-6273(00)80828-4",
language = "English",
volume = "24",
pages = "143--154",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "1",

}

RIS

TY - JOUR

T1 - Endophilin/sh3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis

AU - Ringstad, Niels

AU - Gad, Helge

AU - Löw, Peter

AU - Di Paolo, Gilbert

AU - Brodin, Lennart

AU - Shupliakov, Oleg

AU - De Camilli, Pietro

PY - 1999/1/1

Y1 - 1999/1/1

N2 - Endophilin/SH3p4 is a protein highly enriched in nerve terminals that binds the GTPase dynamin and the polyphosphoinositide phosphatase synaptojanin, two proteins implicated in synaptic vesicle endocytosis. We show here that antibody-mediated disruption of endophilin function in a tonically stimulated synapse leads to a block in the invagination of clathrin-coated pits adjacent to the active zone and therefore to a block of synaptic vesicle recycling. We also show that in a cell-free system, endophilin is not associated with clathrin coats and is a functional partner of dynamin. Our findings suggest that endophilin is part of a biochemical machinery that acts in trans to the clathrin coat from early stages to vesicle fission.

AB - Endophilin/SH3p4 is a protein highly enriched in nerve terminals that binds the GTPase dynamin and the polyphosphoinositide phosphatase synaptojanin, two proteins implicated in synaptic vesicle endocytosis. We show here that antibody-mediated disruption of endophilin function in a tonically stimulated synapse leads to a block in the invagination of clathrin-coated pits adjacent to the active zone and therefore to a block of synaptic vesicle recycling. We also show that in a cell-free system, endophilin is not associated with clathrin coats and is a functional partner of dynamin. Our findings suggest that endophilin is part of a biochemical machinery that acts in trans to the clathrin coat from early stages to vesicle fission.

UR - http://www.scopus.com/inward/record.url?scp=0033199465&partnerID=8YFLogxK

U2 - 10.1016/S0896-6273(00)80828-4

DO - 10.1016/S0896-6273(00)80828-4

M3 - Article

C2 - 10677033

AN - SCOPUS:0033199465

VL - 24

SP - 143

EP - 154

JO - Neuron

JF - Neuron

SN - 0896-6273

IS - 1

ER -

ID: 40835098