RT Journal Article
SR Electronic
T1 Dynamin is primed at endocytic sites for ultrafast endocytosis
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.02.15.431332
DO 10.1101/2021.02.15.431332
A1 Yuuta Imoto
A1 Sumana Raychaudhuri
A1 Pascal Fenske
A1 Eduardo Sandoval
A1 Kie Itoh
A1 Eva-Maria Blumrich
A1 Lauren Mamer
A1 Fereshteh Zarebidaki
A1 Berit Söhl-Kielczynski
A1 Thorsten Trimbuch
A1 Shraddha Nayak
A1 Janet H. Iwasa
A1 Erik M. Jorgensen
A1 Michael A. Cousin
A1 Christian Rosenmund
A1 Shigeki Watanabe
YR 2021
UL http://biorxiv.org/content/early/2021/02/16/2021.02.15.431332.abstract
AB Dynamin mediates fission of vesicles from the plasma membrane during endocytosis. Typically, dynamin is recruited from the cytosol to endocytic sites, requiring seconds to tens of seconds. However, ultrafast endocytosis in neurons internalizes vesicles as quickly as 50 ms during synaptic vesicle recycling. Here we demonstrate that Dynamin 1 is pre-recruited to endocytic sites for ultrafast endocytosis. Specifically, Dynamin 1xA, a splice variant of Dynamin 1, interacts with Syndapin 1 to form molecular condensates on the plasma membrane when the proline-rich domain of this variant is dephosphorylated. When this domain is mutated to include phosphomimetic residues or Syndapin 1’s dynamin-interacting domain is mutated, Dynamin 1xA becomes diffuse, and consequently, ultrafast endocytosis slows down by ∼100-fold. Mechanistically, Syndapin 1 acts as an adaptor by binding the plasma membrane and stores Dynamin 1xA at endocytic sites. This cache bypasses the recruitment step and accelerates endocytosis at synapses.Competing Interest StatementThe authors have declared no competing interest.