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p(HGNC:MAPT, var("?"))

Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Entity

Name
MAPT
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 9

Alzheimer's Disease: Targeting the Cholinergic System v1.0.0

The Ubiquitin Proteasome System in Neurodegenerative Diseases: Sometimes the Chicken, Sometimes the Egg v1.0.0

Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing v1.0.0

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

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0

Protein phosphatase 2A dysfunction in Alzheimer’s disease v1.0.0

Inert and seed-competent tau monomers suggest structural origins of aggregation v1.0.0

Tau in physiology and pathology v1.0.0

In-Edges 9

a(PUBCHEM:10013505) decreases p(HGNC:MAPT, var("?")) View Subject | View Object

Moreover, the M1 agonist AF267B can rescue the cognitive impairment and decrease Aβ42 and tau abnormalities in the cortex and hippocampus of a mouse model of AD PubMed:26813123

Appears in Networks:
Annotations
MeSH
Hippocampus
MeSH
Neocortex
MeSH
Alzheimer Disease

p(HGNC:MAPT) hasVariant p(HGNC:MAPT, var("?")) View Subject | View Object

Appears in Networks:

composite(a(CHEBI:"amyloid-beta"), p(HGNC:MAPT, var("?"))) hasComponent p(HGNC:MAPT, var("?")) View Subject | View Object

Appears in Networks:

a(MESH:Caspases) increases p(HGNC:MAPT, var("?")) View Subject | View Object

Truncation of Tau by caspases and endopeptidases has been suggested to constitute an important pathogenic step in AD PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

a(MESH:Endopeptidases) increases p(HGNC:MAPT, var("?")) View Subject | View Object

Truncation of Tau by caspases and endopeptidases has been suggested to constitute an important pathogenic step in AD PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

path(MESH:"Alzheimer Disease") positiveCorrelation p(HGNC:MAPT, var("?")) View Subject | View Object

Truncation of Tau by caspases and endopeptidases has been suggested to constitute an important pathogenic step in AD PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

p(FPLX:HSP90) regulates p(HGNC:MAPT, var("?")) View Subject | View Object

Together, multiple studies suggest that Hsp90 regulates the stability of both phospho- and mutant-tau PubMed:21882945

Appears in Networks:

p(FPLX:HSP90) increases p(HGNC:MAPT, var("?")) View Subject | View Object

Previous studies have shown that Hsp90 inhibition decreased the levels of hyperphosphorylated and/or mutated tau species both in cells and mice. PubMed:29311797

Appears in Networks:

a(CHEBI:heparin) increases p(HGNC:MAPT, var("?")) View Subject | View Object

After 15 min of heparin exposure, we detected low but significant amounts of seed-compe- tent monomer, and much fewer larger assemblies (Figure 6A). PubMed:29988016

Appears in Networks:

Out-Edges 10

p(HGNC:MAPT, var("?")) decreases act(complex(GO:"proteasome complex")) View Subject | View Object

Both aggregates and mutant forms of tau likewise block the proteasome, and its ability to degrade hyper- phosphorylated and oligomeric tau is reduced compared with its ability to degrade physiological tau 3,55,68 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

p(HGNC:MAPT, var("?")) decreases bp(GO:"chaperone-mediated autophagy") View Subject | View Object

Finally, while physiological tau possesses KFERQ motifs and is degraded by CMA, aggregates, mutant forms and frag- ments interfere with CMA 45,47 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

p(HGNC:MAPT, var("?")) positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

Truncation of Tau by caspases and endopeptidases has been suggested to constitute an important pathogenic step in AD PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

p(HGNC:MAPT, var("?")) increases a(HBP:"Tau aggregates") View Subject | View Object

However, under potentially proteotoxic conditions, the post-translational modifications or mutations that damage tau’s affinity for microtubules and favor its aggregation are thought to generate a molecular ‘danger signal’ that specifically alerts the quality control system [112,113]. PubMed:21882945

Appears in Networks:

p(HGNC:MAPT, var("?")) decreases complex(a(GO:microtubule), p(HGNC:MAPT)) View Subject | View Object

However, under potentially proteotoxic conditions, the post-translational modifications or mutations that damage tau’s affinity for microtubules and favor its aggregation are thought to generate a molecular ‘danger signal’ that specifically alerts the quality control system [112,113]. PubMed:21882945

Appears in Networks:

p(HGNC:MAPT, var("?")) decreases complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:MAPT)) View Subject | View Object

Notably, tau missense mutations found in frontotemporal dementia with Parkinsonism linked to chromosome 17 (FTDP-17; Goedert et al.,2000) and AD-mimicking tau phosphorylation in proline-rich motifs (Eidenmuller et al.,2001) inhibit the association of tau with PP2A (Figure3B). PubMed:24653673

Appears in Networks:

p(HGNC:MAPT, var("?")) increases a(HBP:"Tau aggregates") View Subject | View Object

In familial tauopathies, the mutation of MAPT seems to be the cause of tau aggregation, but in sporadic tauopathies (such as AD), the trigger of tau pathology is unclear. PubMed:26631930

Appears in Networks:

p(HGNC:MAPT, var("?")) increases a(HBP:"Tau aggregates") View Subject | View Object

However Ms induced amyloid forma- tion, albeit more slowly than trimer or unfractionated fibrils (Figure 1F). PubMed:29988016

Appears in Networks:

p(HGNC:MAPT, var("?")) increases tloc(p(HGNC:MAPT), fromLoc(GO:axon), toLoc(MESH:"Dendritic Spines")) View Subject | View Object

Hyperphosphorylation, mutations and overexpression of tau can drive the mislocalization of tau into postsynaptic spines, resulting in synaptic dysfunction PubMed:26631930

Appears in Networks:

p(HGNC:MAPT, var("?")) decreases act(a(GO:synapse)) View Subject | View Object

Hyperphosphorylation, mutations and overexpression of tau can drive the mislocalization of tau into postsynaptic spines, resulting in synaptic dysfunction PubMed:26631930

Appears in Networks:

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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.