Scientific article

Dynamic remodeling of the dynamin helix during membrane constriction

Published inProceedings of the National Academy of Sciences, vol. 114, no. 21, p. 5449-5454
Publication date2017

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.

Citation (ISO format)
COLOM DIEGO, Adai et al. Dynamic remodeling of the dynamin helix during membrane constriction. In: Proceedings of the National Academy of Sciences, 2017, vol. 114, n° 21, p. 5449–5454. doi: 10.1073/pnas.1619578114
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Article (Published version)
ISSN of the journal0027-8424

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