TY  - JOUR
AU  - Kornreich, M.
AU  - Malka-Gibor, E.
AU  - Laser-Azogui, A.
AU  - Doron, O.
AU  - Herrmann, Harald
AU  - Beck, R.
TI  - Composite bottlebrush mechanics: α-internexin fine-tunes neurofilament network properties.
JO  - Soft matter
VL  - 11
IS  - 29
SN  - 1744-6848
CY  - London
PB  - Royal Soc. of Chemistry
M1  - DKFZ-2017-02929
SP  - 5839 - 5849
PY  - 2015
AB  - 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.
KW  - Intermediate Filament Proteins (NLM Chemicals)
KW  - Neurofilament Proteins (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - alpha-internexin (NLM Chemicals)
KW  - Hydrogel (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:26100609
DO  - DOI:10.1039/C5SM00662G
UR  - https://inrepo02.dkfz.de/record/126901
ER  -