p(MGI:Fyn)

Entity

Name

Fyn

Namespace

mgi

Namespace Version

20181021

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/f2f993e599694ab5ce989cc39d789a499f75db99/external/mgi-names.belns

TAU Interactions Section of NESTOR

Tau Modifications Sections of NESTOR

A rapid but transient increase was found in the amount of fyn detected in DRMs on ADDL exposure for 2 min that was partially reduced after 10 min exposure. Mirroring the movement of fyn into the DRM, tau content of DRMs increased in response to ADDLs. To further test a putative association between fyn and tau levels in DRMs, we treated cells with 2-bromopalmitate, an inhibitor of protein palmitoylation, which is required for fyn’s localization in DRMs. This treatment resulted in a progressive reduction in both fyn and tau in DRMs, demonstrating that the association of tau with DRMs may be directly regulated by fyn (Supplemental Fig. 2). PubMed:18096814

A rapid but transient increase was found in the amount of fyn detected in DRMs on ADDL exposure for 2 min that was partially reduced after 10 min exposure. Mirroring the movement of fyn into the DRM, tau content of DRMs increased in response to ADDLs. To further test a putative association between fyn and tau levels in DRMs, we treated cells with 2-bromopalmitate, an inhibitor of protein palmitoylation, which is required for fyn’s localization in DRMs. This treatment resulted in a progressive reduction in both fyn and tau in DRMs, demonstrating that the association of tau with DRMs may be directly regulated by fyn (Supplemental Fig. 2). PubMed:18096814

A rapid but transient increase was found in the amount of fyn detected in DRMs on ADDL exposure for 2 min that was partially reduced after 10 min exposure. Mirroring the movement of fyn into the DRM, tau content of DRMs increased in response to ADDLs. To further test a putative association between fyn and tau levels in DRMs, we treated cells with 2-bromopalmitate, an inhibitor of protein palmitoylation, which is required for fyn’s localization in DRMs. This treatment resulted in a progressive reduction in both fyn and tau in DRMs, demonstrating that the association of tau with DRMs may be directly regulated by fyn (Supplemental Fig. 2). PubMed:18096814

Analysis of synaptosomes revealed that FynCA accumulated at high levels in the spine, resulting in increased levels of the NMDA receptor subunit NR2b phosphorylated at residue Y1472. Tau was strongly phosphorylated at the AT8 epitope S202/T205 as shown by Western blot and immunohistochemistry indicating that an increased tyrosine kinase activity of Fyn has down-stream consequences for serine/threonine-directed phosphorylation. PubMed:25125464

From these findings, it would seem that FYN plays a neuroprotective role. However, FYN may also play a paradoxical role in Abeta toxicity. Indeed, Abeta activates both FYN and the PI3K cascade (Williamson et al., 2002), whereas germline knockout of FYN is neuroprotective in mice (Lambert et al., 1998; Chin et al., 2004). FYN knockout protects mature mouse neurons in organotypic central nervous system cultures (Lambert et al., 1998). PubMed:19293145

A rapid but transient increase was found in the amount of fyn detected in DRMs on ADDL exposure for 2 min that was partially reduced after 10 min exposure. Mirroring the movement of fyn into the DRM, tau content of DRMs increased in response to ADDLs. To further test a putative association between fyn and tau levels in DRMs, we treated cells with 2-bromopalmitate, an inhibitor of protein palmitoylation, which is required for fyn’s localization in DRMs. This treatment resulted in a progressive reduction in both fyn and tau in DRMs, demonstrating that the association of tau with DRMs may be directly regulated by fyn (Supplemental Fig. 2). PubMed:18096814

A rapid but transient increase was found in the amount of fyn detected in DRMs on ADDL exposure for 2 min that was partially reduced after 10 min exposure. Mirroring the movement of fyn into the DRM, tau content of DRMs increased in response to ADDLs. To further test a putative association between fyn and tau levels in DRMs, we treated cells with 2-bromopalmitate, an inhibitor of protein palmitoylation, which is required for fyn’s localization in DRMs. This treatment resulted in a progressive reduction in both fyn and tau in DRMs, demonstrating that the association of tau with DRMs may be directly regulated by fyn (Supplemental Fig. 2). PubMed:18096814

Analysis of synaptosomes revealed that FynCA accumulated at high levels in the spine, resulting in increased levels of the NMDA receptor subunit NR2b phosphorylated at residue Y1472. Tau was strongly phosphorylated at the AT8 epitope S202/T205 as shown by Western blot and immunohistochemistry indicating that an increased tyrosine kinase activity of Fyn has down-stream consequences for serine/threonine-directed phosphorylation. PubMed:25125464

Analysis of synaptosomes revealed that FynCA accumulated at high levels in the spine, resulting in increased levels of the NMDA receptor subunit NR2b phosphorylated at residue Y1472. Tau was strongly phosphorylated at the AT8 epitope S202/T205 as shown by Western blot and immunohistochemistry indicating that an increased tyrosine kinase activity of Fyn has down-stream consequences for serine/threonine-directed phosphorylation. PubMed:25125464

Analysis of synaptosomes revealed that FynCA accumulated at high levels in the spine, resulting in increased levels of the NMDA receptor subunit NR2b phosphorylated at residue Y1472. Tau was strongly phosphorylated at the AT8 epitope S202/T205 as shown by Western blot and immunohistochemistry indicating that an increased tyrosine kinase activity of Fyn has down-stream consequences for serine/threonine-directed phosphorylation. PubMed:25125464