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037 _ _ |a DKFZ-2017-02929
041 _ _ |a eng
082 _ _ |a 530
100 1 _ |a Kornreich, M.
|b 0
245 _ _ |a Composite bottlebrush mechanics: α-internexin fine-tunes neurofilament network properties.
260 _ _ |a London
|c 2015
|b Royal Soc. of Chemistry
336 7 _ |a article
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520 _ _ |a 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.
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650 _ 7 |a Intermediate Filament Proteins
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650 _ 7 |a Neurofilament Proteins
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650 _ 7 |a Recombinant Proteins
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650 _ 7 |a alpha-internexin
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650 _ 7 |a Hydrogel
|0 25852-47-5
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700 1 _ |a Malka-Gibor, E.
|b 1
700 1 _ |a Laser-Azogui, A.
|b 2
700 1 _ |a Doron, O.
|b 3
700 1 _ |a Herrmann, Harald
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700 1 _ |a Beck, R.
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773 _ _ |a 10.1039/C5SM00662G
|g Vol. 11, no. 29, p. 5839 - 5849
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