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Dynamic remodeling of the dynamin helix during membrane constriction.

TitleDynamic remodeling of the dynamin helix during membrane constriction.
Publication TypeJournal Article
Year of Publication2017
AuthorsColom A, Redondo-Morata L, Chiaruttini N, Roux A, Scheuring S
JournalProc Natl Acad Sci U S A
Date Published2017 May 23

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 dynamin helix turns: the average distances between turns reduce with GTP hydrolysis. These distances vary, however, over time because helical turns were observed to transiently pair and dissociate. At fission sites, these cycles of association and dissociation were correlated with relative lateral displacement of the turns and constriction. Our findings show relative longitudinal and lateral displacements of helical turns related to constriction. Our work highlights the potential of high-speed atomic force microscopy for the observation of mechanochemical proteins onto membranes during action at almost molecular resolution.

Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID28484031
PubMed Central IDPMC5448220