1. Catalog
  2. Nodes
  3. a(GO:microtubule)

a(GO:microtubule)

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

Entity

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

Appears in Networks 18

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

Alpha-synuclein oligomers: a new hope v1.0.0

Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5 v1.0.0

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

Adenosine A1 receptor antagonist 64627 alleviates axonopathy caused by human Tau ΔK280 v1.0.0

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

Tau oligomers-Cytotoxicity, propagation, and mitochondrial damage v1.0.0

Tau oligomers-Cytotoxicity, propagation, and mitochondrial damage from Shafiei et al., 2017

Tau oligomers and tau toxicity in neurodegenerative disease v1.0.0

Tau oligomers and tau toxicity in neurodegenerative disease by Ward et al., 2012

Clearance of Amyloid Beta and Tau in Alzheimer’s Disease:from Mechanisms to Therapy v1.0.1

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

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

Alzheimer’s disease and the autophagic-lysosomal system v1.0.0

Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection v1.0.0

Caenorhabditis elegans models of tauopathy v1.0.0

Carboxy terminus heat shock protein 70 interacting protein reduces tau-associated degenerative changes v1.0.0

Tau in physiology and pathology v1.0.0

mTOR-Related Brain Dysfunctions in Neuropsychiatric Disorders v1.0.0

Activity-dependent neuroprotective protein (ADNP) is an alcohol-responsive gene and negative regulator of alcohol consumption in female mice v1.0.0

In-Edges 39

p(HGNC:MAPT) association a(GO:microtubule) View Subject | View Object

In contrast, the neurofibrillary tangles are intracellular and are rich in tau, a structural protein that is normally associated with microtubuli PubMed:14556719

Appears in Networks:

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

Appears in Networks:

complex(a(GO:microtubule), a(MESH:Kinesin)) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

p(HGNC:CDK5) association a(GO:microtubule) View Subject | View Object

Fig. 5 shows that the 31 kDa kinase is included in the MAP fraction after three or more cycles of microtubule assembly (lanes l-6), and is also associated with PHFs (lane 7) PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:ERK) association a(GO:microtubule) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:GSK3) association a(GO:microtubule) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(HGNC:PRKACA) association a(GO:microtubule) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

a(CHEBI:"epothilone A") increases a(GO:microtubule) View Subject | View Object

The microtubule stabilizers paclitaxel and epothilone A countered Aβ42-induced cytoskeletal disruption — and moderated excessive UPR — in neurons 182 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Machado-Joseph Disease

a(CHEBI:"epothilone D") increases a(GO:microtubule) View Subject | View Object

Furthermore, epothilone D countered microtubule disruption and cognitive deficits in aged P301S/P19 AD mice 183 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Machado-Joseph Disease

a(CHEBI:"amyloid-beta polypeptide 42") decreases a(GO:microtubule) View Subject | View Object

The microtubule stabilizers paclitaxel and epothilone A countered Aβ42-induced cytoskeletal disruption — and moderated excessive UPR — in neurons 182 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Machado-Joseph Disease

a(CHEBI:paclitaxel) increases a(GO:microtubule) View Subject | View Object

The microtubule stabilizers paclitaxel and epothilone A countered Aβ42-induced cytoskeletal disruption — and moderated excessive UPR — in neurons 182 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Machado-Joseph Disease

complex(a(GO:microtubule), p(MGI:Mapt)) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

a(HBP:"Tau oligomers") decreases act(a(GO:microtubule)) View Subject | View Object

In fact, tau oligomers might disrupt microtubule stability and trafficking, thus affecting organelle distribution PubMed:28420982

Appears in Networks:
Annotations
MeSH
Extracellular Space
Confidence
High
MeSH
Neurons
MeSH
Alzheimer Disease

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

While functional tau is an unfolded monomeric protein that stabilizes microtubules, regulates neurite growth, and monitors axonal transport of organelles (Medina and Avila, 2014), dysfunctional tau acquires a new toxic function PubMed:28420982

Appears in Networks:
Annotations
Confidence
High

complex(a(GO:microtubule), a(MESH:Dyneins)) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

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

Tau proteins, microtubule-associated proteins, take part in the formation of microtubules for the sake of maintaining the stability of microtubules PubMed:29626319

Appears in Networks:

act(p(HGNC:HDAC6)) negativeCorrelation a(GO:microtubule) View Subject | View Object

Overexpressed tau was hyperphosphorylated and resulted in decreased MT density and greater fragmentation. Using genetic screen, a histone deacetylase 6 (HDAC6) null mutation rescued tau-induced MT defects in both muscles and neurons. Genetic and pharmacological inhibition of the tubulin-specific deacetylase activity of HDAC6 indicates that the rescue effect may be mediated by increased MT acetylation. PubMed:23487739

Appears in Networks:

p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) decreases a(GO:microtubule) View Subject | View Object

Overexpressed tau was hyperphosphorylated and resulted in decreased MT density and greater fragmentation. Using genetic screen, a histone deacetylase 6 (HDAC6) null mutation rescued tau-induced MT defects in both muscles and neurons. Genetic and pharmacological inhibition of the tubulin-specific deacetylase activity of HDAC6 indicates that the rescue effect may be mediated by increased MT acetylation. PubMed:23487739

Appears in Networks:

complex(a(GO:"protein phosphatase type 2A complex"), a(GO:microtubule)) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) regulates a(GO:microtubule) View Subject | View Object

Deregulation of PP2A/Bα alone also affects microtubule stability (Nunbhakdi-Craig et al., 2007) and neurite outgrowth (Sontag et al.,2010) in neuroblastoma cells PubMed:24653673

Appears in Networks:

complex(p(HGNC:PPP2CB), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) regulates a(GO:microtubule) View Subject | View Object

Deregulation of PP2A/Bα alone also affects microtubule stability (Nunbhakdi-Craig et al., 2007) and neurite outgrowth (Sontag et al.,2010) in neuroblastoma cells PubMed:24653673

Appears in Networks:

a(CHEBI:paclitaxel) increases a(GO:microtubule) View Subject | View Object

Paclitaxel reversed Aβ-induced microtubule disruption and restored autophagosomal transport in neurons [161], while a similar compound, epothilone D/BMS-241027, reduced tauopathy and improved cognition in P301S transgenic mice [162] although the compound did not progress beyond Phase I clinical testing PubMed:29758300

Appears in Networks:

complex(a(GO:cytoskeleton), a(GO:microtubule)) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

p(HBP:"Tau isoform D (383 aa)", var("p.Pro301Leu")) decreases a(GO:microtubule) View Subject | View Object

At the later stages, the mutant-tau lines showed microtubule loss and non-apoptotic neuronal death, paralleled by a complete loss of touch response (62). PubMed:29191965

Appears in Networks:

p(HBP:"Tau isoform D (383 aa)", var("p.Arg406Trp")) decreases a(GO:microtubule) View Subject | View Object

At the later stages, the mutant-tau lines showed microtubule loss and non-apoptotic neuronal death, paralleled by a complete loss of touch response (62). PubMed:29191965

Appears in Networks:

bp(GO:"anterograde axonal transport") decreases a(GO:microtubule) View Subject | View Object

This leads to accumulation of mitochondria in the cell body where they cluster near the microtubule center [6]. PubMed:25374103

Appears in Networks:
Annotations
MeSH
Cell Body

p(HGNC:MAPT) regulates act(a(GO:microtubule)) View Subject | View Object

The tau-protein is a natively soluble protein that plays a key role in the dynamics of microtubules PubMed:25374103

Appears in Networks:

complex(a(GO:microtubule), p(HBP:"3R tau")) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

complex(a(GO:microtubule), p(HBP:"4R tau")) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

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

Appears in Networks:

tloc(p(HGNC:MAPT), fromLoc(GO:axon), toLoc(MESH:"Dendritic Spines")) negativeCorrelation a(GO:microtubule) View Subject | View Object

In cultured neurons, missorted dendritic tau may mediate toxicity that is induced by Aβ or other stressors by promoting the translocation of tubulin tyrosine ligase-like enzyme 6 (TTLL6) into dendrites, and the severing of microtubules by spastin PubMed:26631930

Appears in Networks:

complex(a(GO:microtubule), p(HGNC:MAPT, frag("124_441"))) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

complex(a(GO:microtubule), a(MESH:"Microtubule-Associated Proteins")) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

complex(a(GO:microtubule), p(HGNC:DISC1)) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

complex(a(GO:microtubule), p(HGNC:DPYSL2)) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

complex(a(GO:microtubule), p(HGNC:DTNBP1)) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

p(HGNC:MAP2) increases a(GO:microtubule) View Subject | View Object

Among various identified MAPs, microtubule-associated protein 2 (MAP2), which belongs to the MAP2/Tau family, is enriched in the brain and especially in dendrites, where it contributes to microtubule stabilization and overall dendritic architecture. PubMed:30061532

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Dendrites

path(MESH:Schizophrenia) negativeCorrelation act(a(GO:microtubule)) View Subject | View Object

The biological implication behind an impairment of microtubule dynamics is confirmed in post-mortem schizophrenic brain samples, as well as in mouse models of schizophrenia, where mTOR-dependent autophagy dysfunction is accompanied by an altered gene expression and protein levels of the microtubule-associated protein 6 (MAP6) PubMed:30061532

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Schizophrenia

complex(a(GO:microtubule), p(HGNC:ADNP)) hasComponent a(GO:microtubule) View Subject | View Object

Appears in Networks:

Out-Edges 9

a(GO:microtubule) association p(HGNC:MAPT) View Subject | View Object

In contrast, the neurofibrillary tangles are intracellular and are rich in tau, a structural protein that is normally associated with microtubuli PubMed:14556719

Appears in Networks:

a(GO:microtubule) association p(HGNC:PRKACA) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

a(GO:microtubule) association p(FPLX:ERK) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

a(GO:microtubule) association p(HGNC:CDK5) View Subject | View Object

Fig. 5 shows that the 31 kDa kinase is included in the MAP fraction after three or more cycles of microtubule assembly (lanes l-6), and is also associated with PHFs (lane 7) PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

a(GO:microtubule) association p(FPLX:GSK3) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

a(GO:microtubule) negativeCorrelation act(p(HGNC:HDAC6)) View Subject | View Object

Overexpressed tau was hyperphosphorylated and resulted in decreased MT density and greater fragmentation. Using genetic screen, a histone deacetylase 6 (HDAC6) null mutation rescued tau-induced MT defects in both muscles and neurons. Genetic and pharmacological inhibition of the tubulin-specific deacetylase activity of HDAC6 indicates that the rescue effect may be mediated by increased MT acetylation. PubMed:23487739

Appears in Networks:

a(GO:microtubule) increases bp(GO:"autophagosome-lysosome fusion") View Subject | View Object

Microtubule-based vesicular trafficking is essential for delivery of autophagosomes to lysosomes and subsequent fusion [46], and impaired dynein-mediated trafficking is associated with impaired autophagosome/ lysosome fusion and reduced protein turnover [47,48]. PubMed:18930136

Appears in Networks:

a(GO:microtubule) negativeCorrelation tloc(p(HGNC:MAPT), fromLoc(GO:axon), toLoc(MESH:"Dendritic Spines")) View Subject | View Object

In cultured neurons, missorted dendritic tau may mediate toxicity that is induced by Aβ or other stressors by promoting the translocation of tubulin tyrosine ligase-like enzyme 6 (TTLL6) into dendrites, and the severing of microtubules by spastin PubMed:26631930

Appears in Networks:

act(a(GO:microtubule)) negativeCorrelation path(MESH:Schizophrenia) View Subject | View Object

The biological implication behind an impairment of microtubule dynamics is confirmed in post-mortem schizophrenic brain samples, as well as in mouse models of schizophrenia, where mTOR-dependent autophagy dysfunction is accompanied by an altered gene expression and protein levels of the microtubule-associated protein 6 (MAP6) PubMed:30061532

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Schizophrenia

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.