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bp(GO:"actin filament bundle assembly")

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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

Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau v1.0.0

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

p(HGNC:MAPT, frag("244_372")) increases bp(GO:"actin filament bundle assembly") View Subject | View Object

In addition, K18 was capable of bundling F-actin (Supplementary Fig. 5b) PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

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

Appears in Networks:
Annotations
Confidence
High

Out-Edges 0

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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.