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complex(p(HGNC:DCTN1), p(HGNC:MAPT))

Equivalencies: 0 | Classes: 1 | Children: 2 | Explore

Components

Appears in Networks 2

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

Tau in physiology and pathology v1.0.0

In-Edges 6

p(HGNC:MAPT) isA complex(p(HGNC:DCTN1), p(HGNC:MAPT)) View Subject | View Object

Appears in Networks:

p(HGNC:DCTN1) isA complex(p(HGNC:DCTN1), p(HGNC:MAPT)) View Subject | View Object

Appears in Networks:

g(DBSNP:rs63750424) negativeCorrelation complex(p(HGNC:DCTN1), p(HGNC:MAPT)) View Subject | View Object

Mutations of a conserved arginine residue in the Nterminus of tau, found in patients with FTDP-17, affect its binding to dynactin, which is abnormally distributed in the retinal ganglion cell axons of transgenic mice expressing human tau with a mutation in the microtubule-binding domain. PubMed:8391280

Appears in Networks:
Annotations
Uberon
ganglionic layer of retina

p(HGNC:MAPT) directlyIncreases complex(p(HGNC:DCTN1), p(HGNC:MAPT)) View Subject | View Object

Fifth, tau may bind to the p150 subunit of dynactin and thereby facilitate the association of dynactin with microtubules, which stabilizes the interaction of dynein with microtubules and thus supports transport by dynein PubMed:26631930

Appears in Networks:

p(HGNC:MAPT, var("p.Arg5His")) decreases complex(p(HGNC:DCTN1), p(HGNC:MAPT)) View Subject | View Object

Another mutation (R5H or R5L) outside the microtubule-binding domain disrupts the binding of tau to the p150 subunit of the dynactin complex — an essential cofactor for the microtubule motor dynein —thereby possibly interfering with general axonal transport PubMed:26631930

Appears in Networks:

p(HGNC:MAPT, var("p.Arg5Leu")) decreases complex(p(HGNC:DCTN1), p(HGNC:MAPT)) View Subject | View Object

Another mutation (R5H or R5L) outside the microtubule-binding domain disrupts the binding of tau to the p150 subunit of the dynactin complex — an essential cofactor for the microtubule motor dynein —thereby possibly interfering with general axonal transport PubMed:26631930

Appears in Networks:

Out-Edges 5

complex(p(HGNC:DCTN1), p(HGNC:MAPT)) hasComponent p(HGNC:DCTN1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:DCTN1), p(HGNC:MAPT)) hasComponent p(HGNC:MAPT) View Subject | View Object

Appears in Networks:

complex(p(HGNC:DCTN1), p(HGNC:MAPT)) isA p(INTERPRO:"Dynein associated protein") View Subject | View Object

Appears in Networks:

complex(p(HGNC:DCTN1), p(HGNC:MAPT)) negativeCorrelation g(DBSNP:rs63750424) View Subject | View Object

Mutations of a conserved arginine residue in the Nterminus of tau, found in patients with FTDP-17, affect its binding to dynactin, which is abnormally distributed in the retinal ganglion cell axons of transgenic mice expressing human tau with a mutation in the microtubule-binding domain. PubMed:8391280

Appears in Networks:
Annotations
Uberon
ganglionic layer of retina

complex(p(HGNC:DCTN1), p(HGNC:MAPT)) increases complex(a(GO:microtubule), p(HGNC:DCTN1)) View Subject | View Object

Fifth, tau may bind to the p150 subunit of dynactin and thereby facilitate the association of dynactin with microtubules, which stabilizes the interaction of dynein with microtubules and thus supports transport by dynein PubMed:26631930

Appears in Networks:

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.