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Changes in tau phosphorylation in hibernating rodents.

Authors
Type
Published Article
Journal
Journal of Neuroscience Research
1097-4547
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
91
Issue
7
Pages
954–962
Identifiers
DOI: 10.1002/jnr.23220
PMID: 23606524
Source
Medline

Abstract

Tau is a cytoskeletal protein present mainly in the neurons of vertebrates. By comparing the sequence of tau molecule among different vertebrates, it was found that the variability of the N-terminal sequence in tau protein is higher than that of the C-terminal region. The N-terminal region is involved mainly in the binding of tau to cellular membranes, whereas the C-terminal region of the tau molecule contains the microtubule-binding sites. We have compared the sequence of Syrian hamster tau with the sequences of other hibernating and nonhibernating rodents and investigated how differences in the N-terminal region of tau could affect the phosphorylation level and tau binding to cell membranes. We also describe a change, in tau phosphorylation, on a casein kinase 1 (ck1)-dependent site that is found only in hibernating rodents. This ck1 site seems to play an important role in the regulation of tau binding to membranes.

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