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