期刊
BIOPHYSICAL JOURNAL
卷 107, 期 12, 页码 2914-2922出版社
CELL PRESS
DOI: 10.1016/j.bpj.2014.09.050
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类别
资金
- Deutsche Forschungsgemeinschaft (DFG) through the Cluster of Excellence
- DFG Research Center Nano-scale Microscopy and Molecular Physiology of the Brain
- Excellence Initiative
- collaborative research center (Nano-scale Photonic Imaging) [SFB 755]
- [KO 3752/5-1/HE 1853/11-1]
- [HE 1853/11-1]
- [HE 1853/9-2]
Actin filaments, microtubules, and intermediate filaments (IFs) are central elements of the metazoan cytoskeleton. At the molecular level, the assembly mechanism for actin filaments and microtubules is fundamentally different from that of IFs. The former two types of filaments assemble from globular proteins. By contrast, IFs assemble from tetrameric complexes of extended, half-staggered, and antiparallel oriented coiled-coils. These tetramers laterally associate into unit-length filaments; subsequent longitudinal annealing of unit-length filaments yields mature IFs. In vitro, IFs form open structures without a fixed number of tetramers per cross-section along the filament. Therefore, a central question for the structural biology of IFs is whether individual subunits can dissociate from assembled filaments and rebind at other sites. Using the fluorescently labeled IF-protein vimentin for assembly, we directly observe and quantitatively determine subunit exchange events between filaments as well as with soluble vimentin pools. Thereby we demonstrate that the cross-sectional polymorphism of donor and acceptor filaments plays an important role. We propose that in segments of donor filaments with more than the standard 32 molecules per cross-section, subunits are not as tightly bound and are predisposed to be released from the filament.
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