Ontology highlight
ABSTRACT:
SUBMITTER: Colom A
PROVIDER: S-EPMC5448220 | biostudies-literature | 2017 May
REPOSITORIES: biostudies-literature
Colom Adai A Redondo-Morata Lorena L Chiaruttini Nicolas N Roux Aurélien A Scheuring Simon S
Proceedings of the National Academy of Sciences of the United States of America 20170508 21
Dynamin is a dimeric GTPase that assembles into a helix around the neck of endocytic buds. Upon GTP hydrolysis, dynamin breaks these necks, a reaction called membrane fission. Fission requires dynamin to first constrict the membrane. It is unclear, however, how dynamin helix constriction works. Here we undertake a direct high-speed atomic force microscopy imaging analysis to visualize the constriction of single dynamin-coated membrane tubules. We show GTP-induced dynamic rearrangements of the dy ...[more]