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computational model of membrane fission catalyzed by escrt-iii计算模型膜裂变escrt-iii催化
Computational Model of Membrane Fission Catalyzed by
ESCRT-III
1 2 3 3 2
Gur Fabrikant , Suman Lata , James D. Riches , John A. G. Briggs , Winfried Weissenhorn *, Michael M.
Kozlov1*
1 Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel, 2 Unit of Virus Host Cell Interactions (UVHCI) UMR 5233
´
Universite Joseph Fourier-EMBL-CNRS, Grenoble, France, 3 Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany
Abstract
ESCRT-III proteins catalyze membrane fission during multi vesicular body biogenesis, budding of some enveloped viruses and
cell division. We suggest and analyze a novel mechanism of membrane fission by the mammalian ESCRT-III subunits CHMP2
and CHMP3. We propose that the CHMP2-CHMP3 complexes self-assemble into hemi-spherical dome-like structures within the
necks of the initial membrane buds generated by CHMP4 filaments. The dome formation is accompanied by the membrane
attachment to the dome surface, which drives narrowing of the membrane neck and accumulation of the elastic stresses
leading, ultimately, to the neck fission. Based on the bending elastic model of lipid bilayers, we determine the degree of the
membrane attachment to the dome enabling the neck fission and compute the required values of the protein-membrane
binding energy. We estimate the feasible values of this energy and predict a high efficiency for the CHMP2-CHMP3 complexes
in mediating membrane fission. We support the computational model by electron tomography imaging of CHMP2-CHMP3
assemblies in vitro. We predict a high efficiency for the CHMP2-CHMP3 complexes in mediating membrane fission.
Citation: Fabrikant G, Lata S, Riches JD, Briggs JAG, Weissen
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