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Tau protects microtubules in the axon from severing by katanin
Journal article   Open access   Peer reviewed

Tau protects microtubules in the axon from severing by katanin

Liang Qiang, Wenqian Yu, Athena Andreadis, Minhua Luo and Peter W Baas
The Journal of neuroscience, v 26(12), pp 3120-3129
22 Mar 2006
PMID: 16554463
url
https://doi.org/10.1523/JNEUROSCI.5392-05.2006View
Published, Version of Record (VoR) Open

Abstract

Immunohistochemistry Paclitaxel - pharmacology Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism tau Proteins - metabolism Fibroblasts - ultrastructure Microtubules - metabolism Neuronal Plasticity - physiology RNA Interference Axons - ultrastructure Microtubules - ultrastructure Katanin Tauopathies - physiopathology Fibroblasts - metabolism Cell Line Cells, Cultured Adenosine Triphosphatases - metabolism Axons - metabolism Rats Hippocampus - cytology Down-Regulation - physiology Hippocampus - metabolism Tauopathies - metabolism Animals Antineoplastic Agents, Phytogenic - pharmacology Cell Shape - physiology
Microtubules in the axon are more resistant to severing by katanin than microtubules elsewhere in the neuron. We have hypothesized that this is because of the presence of tau on axonal microtubules. When katanin is overexpressed in fibroblasts, the microtubules are severed into short pieces, but this phenomenon is suppressed by the coexpression of tau. Protection against severing is also afforded by microtubule-associated protein 2 (MAP2), which has a tau-like microtubule-binding domain, but not by MAP1b, which has a different microtubule-binding domain. The microtubule-binding domain of tau is required for the protection, but within itself, provides less protection than the entire molecule. When tau (but not MAP2 or MAP1b) is experimentally depleted from neurons, the microtubules in the axon lose their characteristic resistance to katanin. These results, which validate our hypothesis, also suggest a potential explanation for why axonal microtubules deteriorate in neuropathies involving the dissociation of tau from the microtubules.

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Collaboration types
Domestic collaboration
Web of Science research areas
Neurosciences
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