Journal
JOURNAL OF NEUROSCIENCE
Volume 29, Issue 35, Pages 11043-11054Publisher
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.1924-09.2009
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Funding
- Association Francaise contre les Myopathies
- Association pour la Recherche sur le Cancer
- Fonds Europeen de Developement Regional
- Institut National du Cancer
- Canadian Institutes of Health Research
- German National Genome Research Net
- Angers Agglomeration and Association pour la Recherche sur le Cancer
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Neurofilaments assemble from three intermediate-filament proteins, contribute to the radial growth of axons, and are exceptionally stable. Microtubules are dynamic structures that assemble from tubulin dimers to support intracellular transport of molecules and organelles. We show here that neurofilaments, and other intermediate-filament proteins, contain motifs in their N-terminal domains that bind unassembled tubulin. Peptides containing such motifs inhibit the in vitro polymerization of microtubules and can be taken up by cultured cells in which they disrupt microtubules leading to altered cell shapes and an arrest of division. In transgenic mice in which neurofilaments are withheld from the axonal compartment, axonal tubulin accumulation is normal but microtubules assemble in excessive numbers. These observations suggest a model in which axonal neurofilaments modulate local microtubule assembly. This capacity also suggests novel mechanisms through which inherited or acquired disruptions in intermediate filaments might contribute to pathogenesis in multiple conditions.
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