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@ARTICLE{Giani:830009,
author = {Giani, M. and den Otter, W. K. and Briels, Willem},
title = {{E}arly stages of clathrin aggregation at a membrane in
coarse-grained simulations},
journal = {The journal of chemical physics},
volume = {146},
number = {15},
issn = {1089-7690},
address = {Melville, NY},
publisher = {American Institute of Physics},
reportid = {FZJ-2017-03611},
pages = {155102 -},
year = {2017},
abstract = {The self-assembly process of clathrin coated pits during
endocytosis has been simulated by combining and extending
coarse grained models of the clathrin triskelion, the
adaptor protein AP2, and a flexible network membrane. The
AP2’s core, upon binding to membrane and cargo, releases a
motif that can bind clathrin. In conditions where the
core-membrane-cargo binding is weak, the binding of this
motif to clathrin can result in a stable complex. We
characterize the conditions and mechanisms resulting in the
formation of clathrin lattices that curve the membrane,
i.e., clathrin coated pits. The mechanical properties of the
AP2 β linker appear crucial to the orientation of the
curved clathrin lattice relative to the membrane, with
wild-type short linkers giving rise to the inward curving
buds enabling endocytosis while long linkers produce
upside-down cages and outward curving bulges},
cin = {ICS-3},
ddc = {540},
cid = {I:(DE-Juel1)ICS-3-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000399904500036},
doi = {10.1063/1.4979985},
url = {https://juser.fz-juelich.de/record/830009},
}