Send to

Choose Destination
See comment in PubMed Commons below
J Neurosci Res. 2013 Jul;91(7):954-62. doi: 10.1002/jnr.23220. Epub 2013 Apr 19.

Changes in tau phosphorylation in hibernating rodents.

Author information

  • 1Laboratorio Cajal de Circuitos Corticales, Universidad Politécnica de Madrid, Campus Montegancedo, Pozuelo de Alarcón, Spain.


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.

Copyright © 2013 Wiley Periodicals, Inc.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley
    Loading ...
    Write to the Help Desk