endophilin-dynamin complex promotes budding of clathrin-coated vesicles during synaptic vesicle recycling
Clathrin-mediated vesicle recycling in synapses is maintained by a unique set of endocytic proteins and interactions. We show that endophilin localizes in the vesicle pool at rest and in spirals at the necks of clathrin-coated pits (CCPs) during activity in lamprey synapses. Endophilin and dynamin c...
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| Veröffentlicht in: | Journal of cell science 2011-01, Vol.124 (1), p.133-143 |
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| creator | Sundborger, Anna Soderblom, Cynthia Vorontsova, Olga Evergren, Emma Hinshaw, Jenny E Shupliakov, Oleg |
| description | Clathrin-mediated vesicle recycling in synapses is maintained by a unique set of endocytic proteins and interactions. We show that endophilin localizes in the vesicle pool at rest and in spirals at the necks of clathrin-coated pits (CCPs) during activity in lamprey synapses. Endophilin and dynamin colocalize at the base of the clathrin coat. Protein spirals composed of these proteins on lipid tubes in vitro have a pitch similar to the one observed at necks of CCPs in living synapses, and lipid tubules are thinner than those formed by dynamin alone. Tubulation efficiency and the amount of dynamin recruited to lipid tubes are dramatically increased in the presence of endophilin. Blocking the interactions of the endophilin SH3 domain in situ reduces dynamin accumulation at the neck and prevents the formation of elongated necks observed in the presence of GTPγS. Therefore, endophilin recruits dynamin to a restricted part of the CCP neck, forming a complex, which promotes budding of new synaptic vesicles. |
| doi_str_mv | 10.1242/jcs.072686 |
| format | Article |
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We show that endophilin localizes in the vesicle pool at rest and in spirals at the necks of clathrin-coated pits (CCPs) during activity in lamprey synapses. Endophilin and dynamin colocalize at the base of the clathrin coat. Protein spirals composed of these proteins on lipid tubes in vitro have a pitch similar to the one observed at necks of CCPs in living synapses, and lipid tubules are thinner than those formed by dynamin alone. Tubulation efficiency and the amount of dynamin recruited to lipid tubes are dramatically increased in the presence of endophilin. Blocking the interactions of the endophilin SH3 domain in situ reduces dynamin accumulation at the neck and prevents the formation of elongated necks observed in the presence of GTPγS. 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| subjects | Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Animals Clathrin-Coated Vesicles - chemistry Clathrin-Coated Vesicles - genetics Clathrin-Coated Vesicles - metabolism Dynamin I - chemistry Dynamin I - genetics Dynamin I - metabolism Humans Lampreys Petromyzontidae Protein Binding Protein Structure, Tertiary Synapses - chemistry Synapses - genetics Synapses - metabolism Synaptic Vesicles - chemistry Synaptic Vesicles - genetics Synaptic Vesicles - metabolism |
| title | endophilin-dynamin complex promotes budding of clathrin-coated vesicles during synaptic vesicle recycling |
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