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Entity

Name
filamentous actin
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 4

In-Edges 7

composite(complex(GO:"filamentous actin"), p(HGNC:CFL1)) decreases complex(GO:"filamentous actin") View Subject | View Object

One of these binding partners is cofilin, a 21 kDa eukaryotic protein, which binds to F-actin with a Kd < 0.05 μM33 and results in disassembly of F-actin34, 35. Cryo-electron microscopy further showed that the binding site of cofilin on F-actin is highly similar to its binding site on G-actin (Fig. 2a)32 PubMed:29215007

bp(GO:"actin filament polymerization") increases complex(GO:"filamentous actin") View Subject | View Object

We analyzed actin and tau in the PSD-enriched fraction from primary cortical neurons treated with jasplakinolide (Fig. 5E). We observed that increased neuronal F-actin content promotes concurrent tau enrichment (*p0.0150, 2-tailed Student’s t test; control 17.49  0.7755 vs jasplakinolide 27.02  2719, N  4 independent cultures; Fig. 5F). GLUA1, the membrane trafficking of which is known to be actin dependent, was increased (*p 0.0279, 2-tailed Student’s t test; control 16.91  1015 vs jasplakinolide 31.00  4.778, N  4 independent cultures). The amount of Fyn in the PSD was decreased (*p  0.0265, 2-tailed Student’s t test; control 27.25 5.003 vs jasplakinolide 11.71  1.786, N  4 independent cultures). PubMed:24760868

p(HGNC:MAPT) association complex(GO:"filamentous actin") View Subject | View Object

These results show that the amount of tau collected is proportional to neuronal F-actin content, suggesting a close link between F-actin and tau. PubMed:24760868

p(HGNC:MAPT) directlyIncreases complex(GO:"filamentous actin") View Subject | View Object

These results are consistent with previous in vitro studies and indicate that tau induces actin-filament bundling in vitro and F-actin accumulation in vivo, most likely through a direct interaction with F-actin.For genetic analysis, we selected a line of tauV337M-expressing flies that has a moderate rough eye and is a good substrate for genetic modification. Coexpressing an actin transgene (UAS–Act5C–EGFP;GMR– GAL4 driver) markedly enhanced tauV337M-induced toxicity. PubMed:17187063

p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) increases complex(GO:"filamentous actin") View Subject | View Object

In a Drosophila melanogaster model of tauopathy, the hyperphosphorylation of tau led to the abnormal alignment and accumulation of F‑actin filaments, and thereby induced neurodegeneration PubMed:26631930

Out-Edges 4

complex(GO:"filamentous actin") association p(HGNC:MAPT) View Subject | View Object

These results show that the amount of tau collected is proportional to neuronal F-actin content, suggesting a close link between F-actin and tau. PubMed:24760868

complex(GO:"filamentous actin") increases p(HGNC:MAPT) View Subject | View Object

We analyzed actin and tau in the PSD-enriched fraction from primary cortical neurons treated with jasplakinolide (Fig. 5E). We observed that increased neuronal F-actin content promotes concurrent tau enrichment (*p0.0150, 2-tailed Student’s t test; control 17.49  0.7755 vs jasplakinolide 27.02  2719, N  4 independent cultures; Fig. 5F). GLUA1, the membrane trafficking of which is known to be actin dependent, was increased (*p 0.0279, 2-tailed Student’s t test; control 16.91  1015 vs jasplakinolide 31.00  4.778, N  4 independent cultures). The amount of Fyn in the PSD was decreased (*p  0.0265, 2-tailed Student’s t test; control 27.25 5.003 vs jasplakinolide 11.71  1.786, N  4 independent cultures). PubMed:24760868

complex(GO:"filamentous actin") increases p(HGNC:MAPT, loc(GO:synapse)) View Subject | View Object

Together, these results suggest that tau translocation to the synapse depends on the F-actin stabilization that promotes their interaction. PubMed:24760868

complex(GO:"filamentous actin") increases complex(complex(GO:"filamentous actin"), p(HGNC:MAPT)) View Subject | View Object

These results are consistent with previous in vitro studies and indicate that tau induces actin-filament bundling in vitro and F-actin accumulation in vivo, most likely through a direct interaction with F-actin.For genetic analysis, we selected a line of tauV337M-expressing flies that has a moderate rough eye and is a good substrate for genetic modification. Coexpressing an actin transgene (UAS–Act5C–EGFP;GMR– GAL4 driver) markedly enhanced tauV337M-induced toxicity. PubMed:17187063

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

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.