Membrane fission by dynamin: what we know and what we need to know

Bruno Antonny, Christopher Burd, Pietro De Camilli, Elizabeth Chen, Oliver Daumke, Katja Faelber, Marijn Ford, Vadim A. Frolov, Adam Frost, Jenny E. Hinshaw, Tom Kirchhausen, Michael M. Kozlov, Martin Lenz, Harry H. Low, Harvey McMahon, Christien Merrifield, Thomas D. Pollard, Phillip J. Robinson, Aurélien Roux*, Sandra Schmid

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review


The large GTPase dynamin is the first protein shown to catalyze membrane fission. Dynamin and its related proteins are essential to many cell functions, from endocytosis to organelle division and fusion, and it plays a critical role in many physiological functions such as synaptic transmission and muscle contraction. Research of the past three decades has focused on understanding how dynamin works. In this review, we present the basis for an emerging consensus on how dynamin functions. Three properties of dynamin are strongly supported by experimental data: first, dynamin oligomerizes into a helical polymer; second, dynamin oligomer constricts in the presence of GTP; and third, dynamin catalyzes membrane fission upon GTP hydrolysis. We present the two current models for fission, essentially diverging in how GTP energy is spent. We further discuss how future research might solve the remaining open questions presently under discussion.

Original languageEnglish
Pages (from-to)2270-2284
Number of pages15
JournalEMBO Journal
Issue number21
StatePublished - 2 Nov 2016


FundersFunder number
National Institute of General Medical SciencesDP2GM110772
National Institute of Diabetes and Digestive and Kidney DiseasesZIADK060100
National Institute of Neurological Disorders and StrokeR37NS036251
National Center for Advancing Translational SciencesUL1TR001863
Medical Research CouncilMC_U105178795


    • GTPase
    • dynamin
    • endocytosis
    • membrane fission
    • molecular motor


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