FullText URL elife_7_30246.pdf
Author Takeda, Tetsuya| Kozai, Toshiya| Yang, Huiran| Ishikuro, Daiki| Seyama, Kaho| Kumagai, Yusuke| Abe, Tadashi| Yamada, Hiroshi| Uchihashi, Takayuki| Ando, Toshio| Takei, Kohji|
Abstract Dynamin is a mechanochemical GTPase essential for membrane fission during clathrin-mediated endocytosis. Dynamin forms helical complexes at the neck of clathrin-coated pits and their structural changes coupled with GTP hydrolysis drive membrane fission. Dynamin and its binding protein amphiphysin cooperatively regulate membrane remodeling during the fission, but its precise mechanism remains elusive. In this study, we analyzed structural changes of dynamin-amphiphysin complexes during the membrane fission using electron microscopy (EM) and high-speed atomic force microscopy (HS-AFM). Interestingly, HS-AFM analyses show that the dynamin-amphiphysin helices are rearranged to form clusters upon GTP hydrolysis and membrane constriction occurs at protein-uncoated regions flanking the clusters. We also show a novel function of amphiphysin in size control of the clusters to enhance biogenesis of endocytic vesicles. Our approaches using combination of EM and HS-AFM clearly demonstrate new mechanistic insights into the dynamics of dynamin-amphiphysin complexes during membrane fission.
Keywords EM HS-AFM amphiphysin biophysics cell biology dynamin human in vitro reconstitution membrane remodeling structural biology
Published Date 2018-01
Publication Title eLife
Volume volume7
Publisher eLife Sciences Publications
Start Page e30246
ISSN 2050-084X
Content Type Journal Article
language 英語
OAI-PMH Set 岡山大学
File Version publisher
PubMed ID 29357276
DOI 10.7554/eLife.30246
Web of Sience KeyUT 000423036500001
Related Url isVersionOf https://doi.org/10.7554/eLife.30246