期刊
JOURNAL OF CELL SCIENCE
卷 124, 期 1, 页码 133-143出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.072686
关键词
Synapse; Endophilin; Dynamin; Endocytosis
类别
资金
- Swedish Research Council [13473, 20587]
- Linne Center for Developmental Biology and Regenerative Medicine
- Wallenberg's Stiftelse and Hjarnfonden
- NIDDK, NIH
- KI-NIH
- Fernstrom's Stiftelse
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [ZIADK060100, ZIADK060107] Funding Source: NIH RePORTER
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 GTP gamma S. Therefore, endophilin recruits dynamin to a restricted part of the CCP neck, forming a complex, which promotes budding of new synaptic vesicles.
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