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Changes in tau phosphorylation in hibernating rodents
Author(s) -
LeónEspinosa Gonzalo,
García Esther,
GarcíaEscudero Vega,
Hernández Félix,
DeFelipe Javier,
Avila Jesús
Publication year - 2013
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.23220
Subject(s) - phosphorylation , casein kinase 1 , casein kinase 2 , biology , membrane , microtubule , microbiology and biotechnology , sequence (biology) , tau protein , cytoskeleton , binding site , biochemistry , cell , protein kinase c , protein kinase a , medicine , alzheimer's disease , mitogen activated protein kinase kinase , disease
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. © 2013 Wiley Periodicals, Inc.