bp(GO:"retrograde axonal protein transport")

Entity

Name

retrograde axonal protein transport

Namespace

go

Namespace Version

20180921

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

The PAD peptide selectively in- hibited anterograde FAT (Fig. 4 B, D), but not retrograde FAT (Fig. 4B,E). PubMed:21734277

Neither 6D nor 6P tau (Fig. 2D) had an effect on retrograde FAT PubMed:21734277

Neither 6D nor 6P tau (Fig. 2D) had an effect on retrograde FAT PubMed:21734277

Soluble AT8 tau monomers inhibited anterograde FAT (Fig. 6 A, C), while retrograde trans- port was unaffected (Fig. 6 A, D). These data indicate that phos- phorylation of tau at the AT8 epitope, which is associated with hyperphosphorylation of tau in AD and other tauopathies, renders soluble monomeric tau capable of inhibiting antero- grade FAT. PubMed:21734277

Consistent with our model, 􏰁144 –273 tau monomers significantly inhibited antero- grade FAT (Fig. 6 B, C), while retrograde FAT remained unaf- fected (Fig. 6 B, D).Together, these data indicate that disease- associated modifications and mutations in tau that increase exposure of PAD promote activation of the PP1–GSK3 pathway and inhibition of anterograde FAT. PubMed:21734277

As previously reported, perfusion of hT40 monomer had no effect on the rate of anterograde FAT in the squid axoplasm (Fig. 5A), whereas perfusion of hT40 aggregates significantly inhibited anterograde FAT as compared to hT40 monomer (Fig. 5B; Fig. 6A; p = 0.003) (LaPointe et al., 2009b). Neither hT40 monomers nor hT40 aggregates altered the rate of retrograde FAT (Fig. 5A, B; Fig. 6B). PubMed:27373205

As previously reported, perfusion of hT40 monomer had no effect on the rate of anterograde FAT in the squid axoplasm (Fig. 5A), whereas perfusion of hT40 aggregates significantly inhibited anterograde FAT as compared to hT40 monomer (Fig. 5B; Fig. 6A; p = 0.003) (LaPointe et al., 2009b). Neither hT40 monomers nor hT40 aggregates altered the rate of retrograde FAT (Fig. 5A, B; Fig. 6B). PubMed:27373205

In contrast to hT40 monomer, perfusion of S422E monomer selectively inhibited anterograde transport (Fig. 5C; Fig. 6A; p = 0.028), but not retrograde FAT. Surprisingly, aggregated S422E significantly inhibited both anterograde and retrograde FAT rates (Fig. 5D; Fig. 6A, B) compared to S422E monomer (anterograde, p = 0.012; retrograde, p = 0.002) and hT40 aggregates (retrograde only, p = 0.019). PubMed:27373205

In contrast to hT40 monomer, perfusion of S422E monomer selectively inhibited anterograde transport (Fig. 5C; Fig. 6A; p = 0.028), but not retrograde FAT. Surprisingly, aggregated S422E significantly inhibited both anterograde and retrograde FAT rates (Fig. 5D; Fig. 6A, B) compared to S422E monomer (anterograde, p = 0.012; retrograde, p = 0.002) and hT40 aggregates (retrograde only, p = 0.019). PubMed:27373205

Tau serves an important function by enabling microtubules to connect with cytoskeletal components and facilitates anterograde and retrograde axonal transport of vesicles and organelles [39]. PubMed:29758300