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complex(a(GO:"filamentous actin"), p(HGNC:MAPT))

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Components

Appears in Networks 1

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

In-Edges 8

a(HBP:HBP00166) increases complex(a(GO:"filamentous actin"), p(HGNC:MAPT)) View Subject | View Object

The analysis reveals that the proline-rich regions P1–P2 and the four pseudo-repeats contribute to the Tau/F-actin interaction PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

a(HBP:HBP00169) positiveCorrelation complex(a(GO:"filamentous actin"), p(HGNC:MAPT)) View Subject | View Object

The combined data—(i) competition of binding of Tau to F-actin by cofilin, which interacts with actin’s hydrophobic pocket, and (ii) residue-specific PRE effects in the repeat domain of Tau by preferential MTSSL-labeling of C374 in proximity to the hydrophobic pocket—suggest that Tau binds to the solvent-exposed hydrophobic pocket that is located between subdomains 1 and 3 of actin PubMed:29215007

Appears in Networks:
Annotations
Confidence
Medium

p(HGNC:MAPT, pmod(Ph, Ser, 262)) decreases complex(a(GO:"filamentous actin"), p(HGNC:MAPT)) 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, 293)) decreases complex(a(GO:"filamentous actin"), p(HGNC:MAPT)) 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 complex(a(GO:"filamentous actin"), p(HGNC:MAPT)) 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 complex(a(GO:"filamentous actin"), p(HGNC:MAPT)) 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 complex(a(GO:"filamentous actin"), p(HGNC:MAPT)) 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 complex(a(GO:"filamentous actin"), p(HGNC:MAPT)) 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

Out-Edges 3

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

Appears in Networks:

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

Appears in Networks:

complex(a(GO:"filamentous actin"), p(HGNC:MAPT)) positiveCorrelation a(HBP:HBP00169) View Subject | View Object

The combined data—(i) competition of binding of Tau to F-actin by cofilin, which interacts with actin’s hydrophobic pocket, and (ii) residue-specific PRE effects in the repeat domain of Tau by preferential MTSSL-labeling of C374 in proximity to the hydrophobic pocket—suggest that Tau binds to the solvent-exposed hydrophobic pocket that is located between subdomains 1 and 3 of actin PubMed:29215007

Appears in Networks:
Annotations
Confidence
Medium

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.