Dynamin is primed at endocytic sites for ultrafast endocytosis.

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. Single-particle tracking of Dynamin 1xA molecules confirms the liquid-like property of condensates in vivo. When Dynamin 1xA is mutated to disrupt its interaction with Syndapin 1, the condensates do not form, 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. Copyright © 2022 The Author(s). Published by Elsevier Inc. All rights reserved.

Citation

Yuuta Imoto, Sumana Raychaudhuri, Ye Ma, Pascal Fenske, Eduardo Sandoval, Kie Itoh, Eva-Maria Blumrich, Hideaki T Matsubayashi, Lauren Mamer, Fereshteh Zarebidaki, Berit Söhl-Kielczynski, Thorsten Trimbuch, Shraddha Nayak, Janet H Iwasa, Jian Liu, Bin Wu, Taekjip Ha, Takanari Inoue, Erik M Jorgensen, Michael A Cousin, Christian Rosenmund, Shigeki Watanabe. Dynamin is primed at endocytic sites for ultrafast endocytosis. Neuron. 2022 Sep 07;110(17):2815-2835.e13

Mesh Tags

Substances

PMID: 35809574

search → result