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| Home > Publications database > Composite bottlebrush mechanics: α-internexin fine-tunes neurofilament network properties. |
| Home > Publications database > Composite bottlebrush mechanics: α-internexin fine-tunes neurofilament network properties. |
| Journal Article | DKFZ-2017-02929 |
; ; ; ; ;
2015
Royal Soc. of Chemistry
London
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Please use a persistent id in citations: doi:10.1039/C5SM00662G
Abstract: 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.
Keyword(s): Intermediate Filament Proteins ; Neurofilament Proteins ; Recombinant Proteins ; alpha-internexin ; Hydrogel
; Allianz-Lizenz / DFG ; Current Contents - Physical, Chemical and Earth Sciences ; IF < 5 ; JCR ; Nationallizenz
; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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