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a(GO:synapse)

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Entity

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

Appears in Networks 15

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

Role of the nicotinic acetylcholine receptor in Alzheimer's disease pathology and treatment v1.0.1

NACHO Mediates Nicotinic Acetylcholine Receptor Function throughout the Brain v1.0.0

Alzheimer's disease-type neuronal tau hyperphosphorylation induced by A beta oligomers v1.0.0

This document contains the bel code for the Article Alzheimer’s disease-type neuronal tau hyperphosphorylation induced by Abeta oligomers by De Felice et al

Anti-aggregant tau mutant promotes neurogenesis 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 Modifications v1.9.5

Tau Modifications Sections of NESTOR

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

The Ubiquitin–Proteasome System and the Autophagic–Lysosomal System in Alzheimer Disease v1.0.0

Extracellular low-n oligomers of tau cause selective synaptotoxicity without affecting cell viability v1.0.0

Caenorhabditis elegans models of tauopathy v1.0.0

Tau in physiology and pathology v1.0.0

Nuclear Factor Kappa-light-chain-enhancer of Activated B Cells (NF-κB) - a Friend, a Foe, or a Bystander - in the Neurodegenerative Cascade and Pathogenesis of Alzheimer's Disease v1.0.0

mTOR-Related Brain Dysfunctions in Neuropsychiatric Disorders v1.0.0

Activity-dependent neuroprotective protein deficiency models synaptic and developmental phenotypes of autism-like syndrome v1.0.0

In-Edges 36

path(MESH:"Cognitive Dysfunction") negativeCorrelation a(GO:synapse) View Subject | View Object

It has been demonstrated that cholinergic synapses are particularly affected by Aβ oligomers early neurotoxicity [218, 219] and that synaptic loss is the major correlate of cognitive impairment PubMed:26813123

Appears in Networks:

a(CHEBI:"amyloid-beta") decreases a(GO:synapse) View Subject | View Object

The explanation proposed by the authors is that alpha7 nAChR activation through nicotine binding could promote survival pathways and recover the synaptic damage caused by Abeta (Inestrosa et al., 2013) PubMed:25514383

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

act(a(MESH:"alpha7 Nicotinic Acetylcholine Receptor")) increases a(GO:synapse) View Subject | View Object

The explanation proposed by the authors is that alpha7 nAChR activation through nicotine binding could promote survival pathways and recover the synaptic damage caused by Abeta (Inestrosa et al., 2013) PubMed:25514383

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

path(MESH:"Alzheimer Disease") negativeCorrelation a(GO:synapse) View Subject | View Object

Dementia is a debilitating condition frequent in ageing populations, and Alzheimer's Disease (AD) accounts for 70% of all dementia cases. AD is characterized by neuropathological hallmarks consisting of an accumulation of Amyloid beta peptide (Ab) in extracellular plaques, intracellular deposits of tau protein, neuronal loss and, more recently, a prominent synaptic loss was identified (Braak and Braak,1991; Masliah et al., 2001; Selkoe,1991; Spires-Jones and Hyman, 2014) PubMed:25514383

Appears in Networks:

complex(a(GO:synapse), a(HBP:"amyloid-beta derived diffusible ligands")) hasComponent a(GO:synapse) View Subject | View Object

Appears in Networks:

p(HBP:"Tau isoform F (441 aa)", var("p.Lys280del")) decreases a(GO:synapse) View Subject | View Object

This may be due to the strong Tau pathology of the toxic pro-aggregant TauRDΔK leading to Tau aggregation, loss of synapses and loss of neurons PubMed:29202785

Appears in Networks:

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

These tau oligomers potentiate neuronal damage, leading to neurodegeneration and traumatic brain injury (Hawkins et al., 2013; Gerson et al., 2014a, 2016; Sengupta et al., 2015). Moreover, they have been implicated in synaptic loss as shown in studies of wild-type human tau transgenic mice (Spires et al., 2006; Berger et al., 2007; Clavaguera et al., 2013) PubMed:28420982

Appears in Networks:
Annotations
Confidence
High
MeSH
Cerebral Cortex

a(HBP:"Tau oligomers") partOf a(GO:synapse) View Subject | View Object

Appears in Networks:

p(HGNC:MARK4) negativeCorrelation a(GO:synapse) View Subject | View Object

Overexpression of MARK4 led to tau hyperphosphorylation, reduced expression of synaptic markers, and loss of dendritic spines and synapses, phenotypes also observed after Aβ treatment. Importantly, expression of a non-phosphorylatable form of tau with the PAR-1/MARK site mutated blocked the synaptic toxicity induced by MARK4 overexpression or Aβ treatment. To probe the involvement of endogenous MARK kinases in mediating the synaptic toxicity of Aβ, we employed a peptide inhibitor capable of effectively and specifically inhibiting the activities of all PAR-1/MARK family members. This inhibitor abrogated the toxic effects of Aβ oligomers on dendritic spines and synapses as assayed at the morphological and electrophysiological levels. PubMed:22156579

Appears in Networks:
Annotations
Uberon
hippocampal formation

p(RGD:Cdk5r2) positiveCorrelation a(GO:synapse) View Subject | View Object

p39, but not p35, is selectively upregulated by histone acetylation-mediated transcription, underlying the robust increase of Cdk5 activity during rat and mouse neuronal differentiation. Loss of p39 attenuates Cdk5 activity in neurons and preferentially affects phosphorylation of specific Cdk5 targets, leading to aberrant axonal growth and impaired dendritic spine and synapse formation. PubMed:27807169

Appears in Networks:

a(CHEBI:"okadaic acid") decreases a(GO:synapse) View Subject | View Object

In vivo use of phosphatase inhibitors such as okadaic acid has been shown in many studies to induce cognitive impairment and widespread neurotoxic effects that are reminiscent of the hallmark pathological processes occurring in AD pathology, i.e., the accumulation of P-tau, amyloidogenesis, synapse loss and neurodegeneration (Malchiodi-Albedi et al., 1997; Arendt et al., 1998; Sun et al.,2003; Kamat et al.,2013) PubMed:24653673

Appears in Networks:

a(CHEBI:"amyloid-beta") decreases act(a(GO:synapse)) View Subject | View Object

Moreover, administration of UCH-L1 can reverse the amyloid b-protein–induced synaptic dysfunction and memory loss in transgenic mice overexpressing APP and PS1 (Gong et al. 2006). PubMed:22908190

Appears in Networks:

a(HBP:AβOs) decreases act(a(GO:synapse)) View Subject | View Object

Among the various molecular species of Abeta present in the brain, soluble oligomeric forms of Abeta are arguably the most plausible candidates to impair synaptic function (reviewed in Walsh and Selkoe 2004). PubMed:22908190

Appears in Networks:

bp(GO:cognition) positiveCorrelation act(a(GO:synapse)) View Subject | View Object

Synaptic loss has long been documented in AD brain (Gonatas et al. 1967) and, as expected, is strongly correlated with the degree of cognitive impairment (Terry et al. 1991). PubMed:22908190

Appears in Networks:
Annotations
MeSH
Brain

bp(GO:endocytosis) positiveCorrelation act(a(GO:synapse)) View Subject | View Object

Pathological rab5 activation, which in Down syndrome is dependent on bCTF generation (Jiang et al. 2010), can up-regulate endocytosis in a manner functionally equivalent to the elevated endocytosis associated with increased synaptic activity, which is considered a source of Ab generation (Cirrito et al. 2008). PubMed:22908190

Appears in Networks:
Annotations
MeSH
Down Syndrome

p(HGNC:CST3) decreases act(a(GO:synapse)) View Subject | View Object

Similar therapeutic effects, including restoration of synaptic functions, are seen in APP mouse models after deleting cystatin C (Sun et al. 2008), by overexpressing cathepsin B (Mueller-Steiner et al. 2006), or by enhancing its activity (Butler et al. 2011). PubMed:22908190

Appears in Networks:

p(HGNC:CTSB) positiveCorrelation act(a(GO:synapse)) View Subject | View Object

Similar therapeutic effects, including restoration of synaptic functions, are seen in APP mouse models after deleting cystatin C (Sun et al. 2008), by overexpressing cathepsin B (Mueller-Steiner et al. 2006), or by enhancing its activity (Butler et al. 2011). PubMed:22908190

Appears in Networks:

p(HGNC:UCHL1) increases act(a(GO:synapse)) View Subject | View Object

Moreover, administration of UCH-L1 can reverse the amyloid b-protein–induced synaptic dysfunction and memory loss in transgenic mice overexpressing APP and PS1 (Gong et al. 2006). PubMed:22908190

Appears in Networks:

path(MESH:"Alzheimer Disease") negativeCorrelation act(a(GO:synapse)) View Subject | View Object

The earliest symptoms of AD are believed to be due to synaptic dysfunction, and in this context, numerous studies have established a significant role of the UPS in the regulation of synaptic plasticity. PubMed:22908190

Appears in Networks:

path(MESH:"Alzheimer Disease") negativeCorrelation act(a(GO:synapse)) View Subject | View Object

Synaptic loss has long been documented in AD brain (Gonatas et al. 1967) and, as expected, is strongly correlated with the degree of cognitive impairment (Terry et al. 1991). PubMed:22908190

Appears in Networks:
Annotations
MeSH
Brain

p(HBP:"Tau isoform F (441 aa)", var("p.Lys280del")) decreases a(GO:synapse) View Subject | View Object

TauRDΔK comprises the structural elements required for the pathologic assembly of tau filaments, and it causes reversible memory deficits and synapse loss in regulatable transgenic mice [11,25]. PubMed:28528849

Appears in Networks:

p(HBP:"Tau oligomers", var("p.Lys280del")) decreases a(GO:synapse) View Subject | View Object

Tau oligomers from TauRDΔK and TauFLΔK mice reduced the density of the synapses by w50%, whereas tau from wild-type mice had no effect on the density (Fig. 7G). PubMed:28528849

Appears in Networks:

p(HGNC:MAPT) causesNoChange a(GO:synapse) View Subject | View Object

Tau oligomers from TauRDΔK and TauFLΔK mice reduced the density of the synapses by w50%, whereas tau from wild-type mice had no effect on the density (Fig. 7G). PubMed:28528849

Appears in Networks:

p(HGNC:CHRNA7) regulates act(a(GO:synapse)) View Subject | View Object

acr-14 controls body movement by modulating the synaptic inputs and outputs of the ventral cord neural circuitry (83). PubMed:29191965

Appears in Networks:

a(HBP:"Tau aggregates") decreases act(a(GO:synapse)) View Subject | View Object

One exception is the report of the accumulation of tau aggregates in presynaptic boutons in transgenic mice, whereby it induces synaptic dysfunction and loss of presynapses (77). PubMed:29191965

Appears in Networks:
Annotations
MeSH
Presynaptic Terminals

composite(p(HBP:"4R tau", var("p.Lys280del")), p(HBP:"Tau isoform E (412 aa)", var("p.Val337Met"))) decreases a(GO:synapse) View Subject | View Object

As a result, the proaggregant lines showed a range of defects including paralysis, axonal degeneration of GABAergic and cholinergic motor neurons, presynaptic defects, synapse loss, and mitochondrial transport defects early in adulthood PubMed:29191965

Appears in Networks:

tloc(p(HGNC:MAPT), fromLoc(GO:axon), toLoc(GO:"somatodendritic compartment")) decreases act(a(GO:synapse)) View Subject | View Object

First, hyperphosphorylation of tau might induce tau missorting from axons to the somatodendritic compartment, which can cause synaptic dysfunction PubMed:26631930

Appears in Networks:

tloc(p(HGNC:MAPT), fromLoc(GO:axon), toLoc(MESH:"Dendritic Spines")) 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:

p(HGNC:MAPT) negativeCorrelation 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:

p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) 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:

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:

complex(p(HGNC:NFKB1), p(HGNC:RELA)) association a(GO:synapse) View Subject | View Object

Other species of NF-κB have not been found at the synapses suggesting that the synapses contain the p65-p50 heterodimer exclusively PubMed:28745240

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

p(HGNC:DISC1) association a(GO:synapse) View Subject | View Object

This gene encodes for the DISC1 ubiquitous protein, which is implicated in neurogenesis, neuronal migration, axon/dendrite, and synapse formation PubMed:30061532

Appears in Networks:

path(HBP:Neurodegeneration) association act(a(GO:synapse)) View Subject | View Object

In schizophrenia, a progressive synaptic disorder is likely to promote neurodegeneration PubMed:30061532

Appears in Networks:
Annotations
MeSH
Schizophrenia

a(PUBCHEM:9832404) association act(a(GO:synapse)) View Subject | View Object

Additionally, given that ADNP and NAP are linked with autophagy (13), cell adhesion (35), immune response (36), autism (6, 13, 15, 17, 27), and synapse-related processes (6), the analysis included several representative genes pertaining to these processes PubMed:30106381

Appears in Networks:

p(HGNC:ADNP) association act(a(GO:synapse)) View Subject | View Object

Additionally, given that ADNP and NAP are linked with autophagy (13), cell adhesion (35), immune response (36), autism (6, 13, 15, 17, 27), and synapse-related processes (6), the analysis included several representative genes pertaining to these processes PubMed:30106381

Appears in Networks:

Out-Edges 18

a(GO:synapse) negativeCorrelation path(MESH:"Cognitive Dysfunction") View Subject | View Object

It has been demonstrated that cholinergic synapses are particularly affected by Aβ oligomers early neurotoxicity [218, 219] and that synaptic loss is the major correlate of cognitive impairment PubMed:26813123

Appears in Networks:

a(GO:synapse) negativeCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

Dementia is a debilitating condition frequent in ageing populations, and Alzheimer's Disease (AD) accounts for 70% of all dementia cases. AD is characterized by neuropathological hallmarks consisting of an accumulation of Amyloid beta peptide (Ab) in extracellular plaques, intracellular deposits of tau protein, neuronal loss and, more recently, a prominent synaptic loss was identified (Braak and Braak,1991; Masliah et al., 2001; Selkoe,1991; Spires-Jones and Hyman, 2014) PubMed:25514383

Appears in Networks:

act(a(GO:synapse)) regulates p(FPLX:CHRN) View Subject | View Object

At the cellular level, nAChRs can underlie synaptic responses, neuronal excitability, and neurotransmitter release (Dajas-Bailador and Wonnacott, 2004; Gotti and Clementi, 2004; Hogg et al., 2003) PubMed:28445721

Appears in Networks:

a(GO:synapse) positiveCorrelation p(RGD:Cdk5r2) View Subject | View Object

p39, but not p35, is selectively upregulated by histone acetylation-mediated transcription, underlying the robust increase of Cdk5 activity during rat and mouse neuronal differentiation. Loss of p39 attenuates Cdk5 activity in neurons and preferentially affects phosphorylation of specific Cdk5 targets, leading to aberrant axonal growth and impaired dendritic spine and synapse formation. PubMed:27807169

Appears in Networks:

a(GO:synapse) negativeCorrelation p(HGNC:MARK4) View Subject | View Object

Overexpression of MARK4 led to tau hyperphosphorylation, reduced expression of synaptic markers, and loss of dendritic spines and synapses, phenotypes also observed after Aβ treatment. Importantly, expression of a non-phosphorylatable form of tau with the PAR-1/MARK site mutated blocked the synaptic toxicity induced by MARK4 overexpression or Aβ treatment. To probe the involvement of endogenous MARK kinases in mediating the synaptic toxicity of Aβ, we employed a peptide inhibitor capable of effectively and specifically inhibiting the activities of all PAR-1/MARK family members. This inhibitor abrogated the toxic effects of Aβ oligomers on dendritic spines and synapses as assayed at the morphological and electrophysiological levels. PubMed:22156579

Appears in Networks:
Annotations
Uberon
hippocampal formation

act(a(GO:synapse)) negativeCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

The earliest symptoms of AD are believed to be due to synaptic dysfunction, and in this context, numerous studies have established a significant role of the UPS in the regulation of synaptic plasticity. PubMed:22908190

Appears in Networks:

act(a(GO:synapse)) negativeCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

Synaptic loss has long been documented in AD brain (Gonatas et al. 1967) and, as expected, is strongly correlated with the degree of cognitive impairment (Terry et al. 1991). PubMed:22908190

Appears in Networks:
Annotations
MeSH
Brain

act(a(GO:synapse)) positiveCorrelation bp(GO:cognition) View Subject | View Object

Synaptic loss has long been documented in AD brain (Gonatas et al. 1967) and, as expected, is strongly correlated with the degree of cognitive impairment (Terry et al. 1991). PubMed:22908190

Appears in Networks:
Annotations
MeSH
Brain

act(a(GO:synapse)) decreases path(MESH:"Plaque, Amyloid") View Subject | View Object

In transgenic mouse models of AD, synaptic deficits have been detected prior to the formation of amyloid plaques (Hsia et al. 1999). PubMed:22908190

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

act(a(GO:synapse)) positiveCorrelation bp(GO:endocytosis) View Subject | View Object

Pathological rab5 activation, which in Down syndrome is dependent on bCTF generation (Jiang et al. 2010), can up-regulate endocytosis in a manner functionally equivalent to the elevated endocytosis associated with increased synaptic activity, which is considered a source of Ab generation (Cirrito et al. 2008). PubMed:22908190

Appears in Networks:
Annotations
MeSH
Down Syndrome

act(a(GO:synapse)) positiveCorrelation p(HGNC:CTSB) View Subject | View Object

Similar therapeutic effects, including restoration of synaptic functions, are seen in APP mouse models after deleting cystatin C (Sun et al. 2008), by overexpressing cathepsin B (Mueller-Steiner et al. 2006), or by enhancing its activity (Butler et al. 2011). PubMed:22908190

Appears in Networks:

act(a(GO:synapse)) increases tloc(p(HGNC:MAPT), fromLoc(GO:"dendritic shaft"), toLoc(GO:"excitatory synapse")) View Subject | View Object

To date, the physiological function of dendritic tau has not been well characterized. It may be involved in the regulation of synaptic plasticity, as pharmacological synaptic activation induces translocation of endogenous tau from the dendritic shaft to excitatory postsynaptic compartments in cultured mouse neurons and in acute hippocampal slices PubMed:26631930

Appears in Networks:
Annotations
MeSH
Dendritic Spines

act(a(GO:synapse)) negativeCorrelation p(HGNC:MAPT) 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:

a(GO:synapse) association complex(p(HGNC:NFKB1), p(HGNC:RELA)) View Subject | View Object

Other species of NF-κB have not been found at the synapses suggesting that the synapses contain the p65-p50 heterodimer exclusively PubMed:28745240

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

act(a(GO:synapse)) association path(HBP:Neurodegeneration) View Subject | View Object

In schizophrenia, a progressive synaptic disorder is likely to promote neurodegeneration PubMed:30061532

Appears in Networks:
Annotations
MeSH
Schizophrenia

a(GO:synapse) association p(HGNC:DISC1) View Subject | View Object

This gene encodes for the DISC1 ubiquitous protein, which is implicated in neurogenesis, neuronal migration, axon/dendrite, and synapse formation PubMed:30061532

Appears in Networks:

act(a(GO:synapse)) association p(HGNC:ADNP) View Subject | View Object

Additionally, given that ADNP and NAP are linked with autophagy (13), cell adhesion (35), immune response (36), autism (6, 13, 15, 17, 27), and synapse-related processes (6), the analysis included several representative genes pertaining to these processes PubMed:30106381

Appears in Networks:

act(a(GO:synapse)) association a(PUBCHEM:9832404) View Subject | View Object

Additionally, given that ADNP and NAP are linked with autophagy (13), cell adhesion (35), immune response (36), autism (6, 13, 15, 17, 27), and synapse-related processes (6), the analysis included several representative genes pertaining to these processes PubMed:30106381

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.