%0 Journal Article
%A Kornreich, M.
%A Malka-Gibor, E.
%A Laser-Azogui, A.
%A Doron, O.
%A Herrmann, Harald
%A Beck, R.
%T Composite bottlebrush mechanics: α-internexin fine-tunes neurofilament network properties.
%J Soft matter
%V 11
%N 29
%@ 1744-6848
%C London
%I Royal Soc. of Chemistry
%M DKFZ-2017-02929
%P 5839 - 5849
%D 2015
%X Neuronal cytoplasmic intermediate filaments are principal structural and mechanical elements of the axon. Their expression during embryonic development follows a differential pattern, while their unregulated expression is correlated to neurodegenerative diseases. The largest neurofilament proteins of medium (NF-M) and high molecular weight (NF-H) were shown to modulate the axonal architecture and inter-filament spacing. However, the individual roles of the remaining α-internexin (α-Inx) and neurofilament of low molecular weight (NF-L) proteins in composite filaments remained elusive. In contrast to previous predictions, we show that when co-assembled with NF-M, the shortest and the least charged α-Inx protein increases inter-filament spacing. These findings suggest a novel structural explanation for the expression pattern of neurofilament proteins during embryonic development. We explain our results by an analysis of ionic cross-links between the disordered polyampholytic C-terminal tails and suggest that a collapsed conformation of the α-Inx tail domain interferes with tail cross-linking near the filament backbone.
%K Intermediate Filament Proteins (NLM Chemicals)
%K Neurofilament Proteins (NLM Chemicals)
%K Recombinant Proteins (NLM Chemicals)
%K alpha-internexin (NLM Chemicals)
%K Hydrogel (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:26100609
%R 10.1039/C5SM00662G
%U https://inrepo02.dkfz.de/record/126901