Document Type
Journal ArticlePublication Date
2006-03-24Keywords
Adenosine TriphosphatasesAnimals
Antineoplastic Agents, Phytogenic
Axons
Cell Line
Cell Shape
Cells, Cultured
Down-Regulation
Fibroblasts
Hippocampus
Immunohistochemistry
Microtubule-Associated Proteins
Microtubules
Neuronal Plasticity
Paclitaxel
RNA Interference
Rats
Tauopathies
tau Proteins
Cell Biology
Metadata
Show full item recordAbstract
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.Source
J Neurosci. 2006 Mar 22;26(12):3120-9. Link to article on publisher's siteDOI
10.1523/JNEUROSCI.5392-05.2006Permanent Link to this Item
http://hdl.handle.net/20.500.14038/25693PubMed ID
16554463Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1523/JNEUROSCI.5392-05.2006