complex(p(HGNC:FYN), p(HGNC:MAPT))

Components

• p(HGNC:FYN)
• p(HGNC:MAPT)

TAU Interactions Section of NESTOR

FYN physically interacts with and phosphorylates tau protein, and the affinity of this physical interaction is enhanced in AD-associated mutations in tau protein (Bhaskar et al., 2005). Abeta rapidly induces tyrosine phosphorylation of many proteins (including tau protein) in human and cultured rat cortical neurons (Williamson et al., 2002). This phosphorylation is concomitant with phosphorylation and inactivation of focal adhesion kinase 1 (FADK1, a major downstream target of FYN), is blocked by inhibitors of SRC kinases and PI3K, and involves FYN associating physically with FADK1 (Williamson et al., 2002). PubMed:19293145

The interaction of tau with FYN may regulate the postsynaptic targeting of FYN, and thereby mediate Aβ‑induced excitotoxicity PubMed:26631930

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. PubMed:18680553

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. PubMed:18680553

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. PubMed:18680553

Conversely, decreased PP2A methylation and PP2A/Bα levels in AD will disrupt normal PP2A-tau interactions (Sontag et al., 2007), thereby preventing PP2A-mediated tau dephosphorylation while allowing for enhanced binding of Fyn kinase or other regulators to the tau proteins. PubMed:24653673

FYN physically interacts with and phosphorylates tau protein, and the affinity of this physical interaction is enhanced in AD-associated mutations in tau protein (Bhaskar et al., 2005). Abeta rapidly induces tyrosine phosphorylation of many proteins (including tau protein) in human and cultured rat cortical neurons (Williamson et al., 2002). This phosphorylation is concomitant with phosphorylation and inactivation of focal adhesion kinase 1 (FADK1, a major downstream target of FYN), is blocked by inhibitors of SRC kinases and PI3K, and involves FYN associating physically with FADK1 (Williamson et al., 2002). PubMed:19293145

The interaction of tau with FYN may regulate the postsynaptic targeting of FYN, and thereby mediate Aβ‑induced excitotoxicity PubMed:26631930

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. PubMed:18680553

Conversely, decreased PP2A methylation and PP2A/Bα levels in AD will disrupt normal PP2A-tau interactions (Sontag et al., 2007), thereby preventing PP2A-mediated tau dephosphorylation while allowing for enhanced binding of Fyn kinase or other regulators to the tau proteins. PubMed:24653673