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bp(GO:"anterograde axonal protein transport")

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Entity

Name
anterograde axonal protein transport
Namespace
go
Namespace Version
20181221
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/73688d6dc24e309fca59a1340dc9ee971e9f3baa/external/go-names.belns

Appears in Networks 6

APP processing in Alzheimer's disease v1.0.1

APP processing in Alzheimer's disease

Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases. v1.0.0

Tau oligomers-Cytotoxicity, propagation, and mitochondrial damage v1.0.0

Tau oligomers-Cytotoxicity, propagation, and mitochondrial damage from Shafiei et al., 2017

Pseudophosphorylation of tau at S422 enhances SDS-stable dimer formation and impairs both anterograde and retrograde fast axonal transport. v1.0.0

Tau oligomers and tau toxicity in neurodegenerative disease v1.0.0

Tau oligomers and tau toxicity in neurodegenerative disease by Ward et al., 2012

Alzheimer’s disease and the autophagic-lysosomal system v1.0.0

In-Edges 26

p(HGNC:APP) association bp(GO:"anterograde axonal protein transport") View Subject | View Object

APP undergoes rapid anterograde transport in neurons PubMed:21214928

Appears in Networks:
Annotations
Confidence
High
MeSH
Neurons

p(HBP:"6D tau", frag("2_18")) association bp(GO:"anterograde axonal protein transport") View Subject | View Object

As observed with 􏰁2–18 tau aggregates (LaPointe et al., 2009), monomeric 􏰁2–18 6D tau showed no effect on FAT (Fig. 4 A, D), demonstrating that PAD is necessary for 6D tau- mediated inhibition of anterograde FAT. PubMed:21734277

Appears in Networks:

p(HBP:"6D tau", frag("2_18")) increases bp(GO:"anterograde axonal protein transport") View Subject | View Object

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

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p(HBP:"6D tau", frag("2_18")) increases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Collectively, these data indicate that PAD is both necessary and sufficient to inhibit an- terograde FAT by activating the PP1–GSK3 cascade. PubMed:21734277

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p(HBP:"6D tau") decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

perfusion of full-length WT tau monomers (2 􏰊M) (Fig. 1 A) had no effect on FAT in squid axoplasm (Fig. 2 A), while 6D and 6P tau monomers (2 􏰊M) significantly inhibited anterograde FAT when compared with WT tau monomer (Fig. 2 B, C) or buf- fer controls (data not shown). PubMed:21734277

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p(HBP:"6D tau") decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Together, these data demonstrate that, as posited for aggregated tau (LaPointe et al., 2009), short N-terminal isoforms of tau inhibit anterograde FAT by a mech- anism involving activation of PP1 and GSK3 that is independent of microtubule binding. PubMed:21734277

Appears in Networks:

p(HBP:"6P tau") decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

perfusion of full-length WT tau monomers (2 􏰊M) (Fig. 1 A) had no effect on FAT in squid axoplasm (Fig. 2 A), while 6D and 6P tau monomers (2 􏰊M) significantly inhibited anterograde FAT when compared with WT tau monomer (Fig. 2 B, C) or buf- fer controls (data not shown). PubMed:21734277

Appears in Networks:

p(HBP:"AT8 tau") decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

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

Appears in Networks:

p(HBP:"delta 144-273 tau") decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

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

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act(p(MESH:"Glycogen Synthase Kinase 3")) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Together, these data demonstrate that, as posited for aggregated tau (LaPointe et al., 2009), short N-terminal isoforms of tau inhibit anterograde FAT by a mech- anism involving activation of PP1 and GSK3 that is independent of microtubule binding. PubMed:21734277

Appears in Networks:

act(p(MESH:"Protein Phosphatase 1")) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Together, these data demonstrate that, as posited for aggregated tau (LaPointe et al., 2009), short N-terminal isoforms of tau inhibit anterograde FAT by a mech- anism involving activation of PP1 and GSK3 that is independent of microtubule binding. PubMed:21734277

Appears in Networks:

a(HBP:"Tau aggregates") decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Additionally, studies have discovered that aggregated tau inhibits fast axonal transport in the anterograde direction at all physiological tau levels, whereas tau monomers have had no effect in either direction (LaPointe et al., 2009; Morfini et al., 2009) PubMed:28420982

Appears in Networks:
Annotations
Confidence
High
MeSH
Cerebral Cortex

composite(a(HBP:"Tau aggregates"), p(HGNC:MAPT)) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

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

Appears in Networks:

p(HGNC:MAPT) causesNoChange bp(GO:"anterograde axonal protein transport") View Subject | View Object

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

Appears in Networks:

composite(a(HBP:"Tau aggregates"), p(HGNC:MAPT, var("p.S422E"))) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

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

Appears in Networks:

p(HGNC:MAPT, var("p.S422E")) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

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

Appears in Networks:

a(HBP:"Tau aggregates") decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Using a squid axoplasm assay, we have demonstrated that aggregated tau inhibits anterograde FAT (fast axonal transport), whereas monomeric tau has no effect PubMed:22817713

Appears in Networks:
Annotations
Confidence
High
MeSH
Intracellular Space

a(HBP:"Tau aggregates") decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

We discovered that aggregated tau inhibits FAT only in the anterograde direction at physiological tau levels, whereas tau monomers had no effect on FAT in either direction, even at concentrations of tau >10-fold higher than PubMed:22817713

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Intracellular Space

a(HBP:"Tau aggregates") decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

However, when tau aggregates, this conformation is altered, exposing PAD and allowing activation of the PP1/GSK3 signalling pathway facilitating FAT inhibition [21] PubMed:22817713

Appears in Networks:
Annotations
Confidence
High
MeSH
Intracellular Space

complex(a(HBP:"Tau oligomers"), p(HGNC:HSPA1A)) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

We illustrate that Hsp70 preferentially binds to tau oligomers over filaments and prevents anterograde FAT inhibition observed with a mixture of both forms of aggregated tau PubMed:22817713

Appears in Networks:
Annotations
Confidence
High
MeSH
Intracellular Space

complex(a(HBP:"Tau oligomers"), p(HGNC:HSPA1A)) increases bp(GO:"anterograde axonal protein transport") View Subject | View Object

However, our data indicate that Hsp70 preferentially binds to oligomeric as opposed to fibrillar tau aggregates and prevents anterograde FAT inhibition [31] PubMed:22817713

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Intracellular Space

composite(p(HGNC:HSPA1A), p(HGNC:MAPT, frag("2_18"))) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Furthermore, when Hsp70 was pre-incubated with the PAD peptide and introduced to the squid axoplasm, inhibition of FAT was still observed [31] PubMed:22817713

Appears in Networks:
Annotations
Confidence
High
MeSH
Intracellular Space

p(HGNC:MAPT, frag("2_18")) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Deletion analyses demonstrate that FAT inhibition requires a small stretch of amino acids (residues 2–18) located within the N-terminus that we have termed the PAD (phosphataseactivation domain) [21] PubMed:22817713

Appears in Networks:
Annotations
Confidence
Low
MeSH
Intracellular Space

p(HGNC:GSK3A) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Further investigation illustrated that this inhibition occurs via activation of a signalling cascade involving PP1 (protein phosphatase 1) and GSK3 (glycogen synthase kinase 3) [24] PubMed:22817713

Appears in Networks:
Annotations
Confidence
High
MeSH
Intracellular Space

p(HGNC:PPP1CA) decreases bp(GO:"anterograde axonal protein transport") View Subject | View Object

Further investigation illustrated that this inhibition occurs via activation of a signalling cascade involving PP1 (protein phosphatase 1) and GSK3 (glycogen synthase kinase 3) [24] PubMed:22817713

Appears in Networks:
Annotations
Confidence
High
MeSH
Intracellular Space

p(HGNC:MAPT) increases bp(GO:"anterograde axonal protein transport") View Subject | View Object

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

Appears in Networks:

Out-Edges 2

bp(GO:"anterograde axonal protein transport") association p(HGNC:APP) View Subject | View Object

APP undergoes rapid anterograde transport in neurons PubMed:21214928

Appears in Networks:
Annotations
Confidence
High
MeSH
Neurons

bp(GO:"anterograde axonal protein transport") association p(HBP:"6D tau", frag("2_18")) View Subject | View Object

As observed with 􏰁2–18 tau aggregates (LaPointe et al., 2009), monomeric 􏰁2–18 6D tau showed no effect on FAT (Fig. 4 A, D), demonstrating that PAD is necessary for 6D tau- mediated inhibition of anterograde FAT. PubMed:21734277

Appears in Networks:

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.