An endophilin-dynamin complex promotes budding of clathrin-coated vesicles during synaptic vesicle recycling

Anna Sundborger, Cynthia Soderblom, Olga Vorontsova, Emma Evergren, Jenny E Hinshaw, Oleg Shupliakov

Research output: Contribution to journalArticlepeer-review

89 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)133-43
Number of pages11
JournalJournal of Cell Science
Volume124
Issue numberPt 1
DOIs
Publication statusPublished - 01 Jan 2011

Keywords

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Clathrin-Coated Vesicles
  • Dynamin I
  • Humans
  • Lampreys
  • Protein Binding
  • Protein Structure, Tertiary
  • Synapses
  • Synaptic Vesicles

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