TY - JOUR

T1 - An endophilin-dynamin complex promotes budding of clathrin-coated vesicles during synaptic vesicle recycling

AU - Sundborger, Anna

AU - Soderblom, Cynthia

AU - Vorontsova, Olga

AU - Evergren, Emma

AU - Hinshaw, Jenny E.

AU - Shupliakov, Oleg

PY - 2011/1/1

Y1 - 2011/1/1

N2 - 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.

AB - 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.

KW - Dynamin

KW - Endocytosis

KW - Endophilin

KW - Synapse

UR - http://www.scopus.com/inward/record.url?scp=78651100928&partnerID=8YFLogxK

U2 - 10.1242/jcs.072686

DO - 10.1242/jcs.072686

M3 - Article

C2 - 21172823

AN - SCOPUS:78651100928

VL - 124

SP - 133

EP - 143

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 1

ER -