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Entity

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

Appears in Networks 1

In-Edges 15

p(HGNC:MAPT) increases bp(GO:"actin filament bundle assembly") View Subject | View Object

Addition of an equimolar concentration of Tau caused bundling of F-actin (Fig. 1b), although some single filaments remained PubMed:29215007

p(HGNC:MAPT) increases bp(GO:"actin filament bundle assembly") View Subject | View Object

Quantification of the intensity of different bands indicated that ~63% of Tau remained in the supernatant. In addition, ~8% of Tau molecules were bound to single filaments, while ~29% of Tau was found together with actin bundles. The data demonstrate that Tau bundles actin filaments PubMed:29215007

p(HGNC:MAPT, frag("254_268")) decreases bp(GO:"actin filament bundle assembly") View Subject | View Object

In contrast to Tau(254–290), however, Tau(254–268) was not able to bundle F-actin (Supplementary Fig. 5d) PubMed:29215007

p(HGNC:MAPT, frag("254_290")) increases bp(GO:"actin filament bundle assembly") View Subject | View Object

To gain insight into the structure, which these segments adopt in complex with F-actin, we used the peptide Tau(254–290), which bundles filaments (Fig. 3a) PubMed:29215007

p(HGNC:MAPT, frag("254_290")) increases bp(GO:"actin filament bundle assembly") View Subject | View Object

In contrast to Tau(254–290), however, Tau(254–268) was not able to bundle F-actin (Supplementary Fig. 5d) PubMed:29215007

p(HGNC:MAPT, frag("292_319")) increases bp(GO:"actin filament bundle assembly") View Subject | View Object

Tau(292–319) comprises the residues of repeat R2 and R3, which experience strong signal attenuation upon addition of F-actin to full-length Tau (Fig. 1e, f). In agreement with the ability of Tau(292–319) to bind to F-actin, the peptide promotes bundling of actin filaments (Supplementary Fig. 5c) PubMed:29215007

p(HGNC:MAPT, pmod(Ph, Ser, 262)) decreases bp(GO:"actin filament bundle assembly") View Subject | View Object

The NMR experiments demonstrate that MARK2- phosphorylation of Tau attenuates its binding to F-actin. Consistent with a reduced affinity, MARK2-phosphorylated Tau failed in bundling actin filaments (Fig. 4e) PubMed:29215007

p(HGNC:MAPT, pmod(Ph, Ser, 262)) decreases bp(GO:"actin filament bundle assembly") View Subject | View Object

In addition, attachment of a phosphate group to S262 in the peptide Tau (254–284) decreased the affinity of the peptide for F-actin (Supplementary Fig. 1) and lowered the amount of Tau (254–284)-promoted actin bundles (Fig. 4f) PubMed:29215007

p(HGNC:MAPT, pmod(Ph, Ser, 293)) decreases bp(GO:"actin filament bundle assembly") View Subject | View Object

The NMR experiments demonstrate that MARK2- phosphorylation of Tau attenuates its binding to F-actin. Consistent with a reduced affinity, MARK2-phosphorylated Tau failed in bundling actin filaments (Fig. 4e) PubMed:29215007

p(HGNC:MAPT, pmod(Ph, Ser, 305)) decreases bp(GO:"actin filament bundle assembly") View Subject | View Object

The NMR experiments demonstrate that MARK2- phosphorylation of Tau attenuates its binding to F-actin. Consistent with a reduced affinity, MARK2-phosphorylated Tau failed in bundling actin filaments (Fig. 4e) PubMed:29215007

p(HGNC:MAPT, pmod(Ph, Ser, 324)) decreases bp(GO:"actin filament bundle assembly") View Subject | View Object

The NMR experiments demonstrate that MARK2- phosphorylation of Tau attenuates its binding to F-actin. Consistent with a reduced affinity, MARK2-phosphorylated Tau failed in bundling actin filaments (Fig. 4e) PubMed:29215007

p(HGNC:MAPT, pmod(Ph, Ser, 356)) decreases bp(GO:"actin filament bundle assembly") View Subject | View Object

The NMR experiments demonstrate that MARK2- phosphorylation of Tau attenuates its binding to F-actin. Consistent with a reduced affinity, MARK2-phosphorylated Tau failed in bundling actin filaments (Fig. 4e) PubMed:29215007

p(HGNC:MAPT, pmod(Ph, Ser, 416)) decreases bp(GO:"actin filament bundle assembly") View Subject | View Object

The NMR experiments demonstrate that MARK2- phosphorylation of Tau attenuates its binding to F-actin. Consistent with a reduced affinity, MARK2-phosphorylated Tau failed in bundling actin filaments (Fig. 4e) PubMed:29215007

p(HGNC:MAPT, var("p.Leu256Glu")) decreases bp(GO:"actin filament bundle assembly") View Subject | View Object

In agreement with a decrease in affinity of Tau(254–290)-L266E for binding to F-actin (Supplementary Fig. 1), the mutant peptide was less efficient in promoting F-actin bundling (Supplementary Fig. 10f) PubMed:29215007

Out-Edges 0

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.