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

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Item Type:Review
Title:Membrane fission by dynamin: what we know and what we need to know
Creators Name:Antonny, B. and Burd, C. and De Camilli, P. and Chen, E. and Daumke, O. and Faelber, K. and Ford, M. and Frolov, V.A. and Frost, A. and Hinshaw, J.E. and Kirchhausen, T. and Kozlov, M.M. and Lenz, M. and Low, H.H. and McMahon, H. and Merrifield, C. and Pollard, T.D. and Robinson, P.J. and Roux, A. and Schmid, S.
Abstract: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.
Keywords:Dynamin, Membrane Fission, Endocytosis, GTPase, Molecular Motor, Animals
Source:EMBO Journal
ISSN:0261-4189
Publisher:EMBO Press / Wiley-Blackwell (U.S.A.)
Volume:35
Number:21
Page Range:2270-2284
Date:2 November 2016
Official Publication:https://doi.org/10.15252/embj.201694613
PubMed:View item in PubMed

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