PubMed: 18680553

Title
Truncated Tau with the Fyn-binding domain and without the microtubule-binding domain hinders the myelinating capacity of an oligodendrocyte cell line.
Journal
Journal of neurochemistry
Volume
107
Issue
None
Pages
351-60
Date
2008-10-01
Authors
LoPresti P | Belkadi A

Evidence 98c5251bf6

Here we demonstrate that the Tau-Fyn interaction has a role in developmental myelination. CG-4 cells were stably transfected with control and experimental truncated Tau and transplanted in the brain and spinal cord of the md rats. In the brain, experimental cells have a severe defect in their ability to extend cellular processes and form myelin; in the spinal cord the cells extend cellular processes but the extent of myelination rostral and caudal to the injection site was decreased compared to control. Cultured experimental cells display shorter cellular process length. In addition experimental cells have Fyn largely in the cell body, whereas control cells distribute Fyn both in the cell body and the processes. Taken together these results demonstrate a direct effect of Tau in OLGs in in vivo myelination.

Evidence 298619af25

Furthermore, Tau binds Fyn both in neuronal and oligodendroglial cells (Brandt et al. 1995; Klein et al.2002), and Fyn phosphorylates Tau in neuronal cells (Lee et al. 2004). The main Fyn SH3 domain-binding PXXP motif (Pro, Lys, Ser, Pro) in adult rat Tau is at the residues 223-226 (Kosik et al. 1989; Lee et al. 1998).

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