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Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 11

a(CHEBI:"amyloid-beta") increases p(HGNC:MARK4) View Subject | View Object

Consistent with previous reports (11,34), treatment of rat hippocampal neurons with synthetic Aβ, prepared using a well-characterized procedure that enriches for Aβ oligomers (37), resulted in increased tau phosphorylation at the 12E8 sites (Fig. 2A), suggesting that Aβ treatment had activated MARK kinases. Increased phosphorylation of tau at a site recognized by the PHF-1 phospho-tau antibody was also observed (data not shown). PubMed:22156579

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Uberon
hippocampal formation

a(CHEBI:"methylene blue") decreases act(p(HGNC:MARK4), ma(kin)) View Subject | View Object

In 293T culture, MB decreased MARK4-mediated Tau phosphorylation in a dose dependent manner. MB down-regulates MARK4 protein level through ubiquitin-proteasome pathway and inhibition of MARK4 kinase activity in vitro. PubMed:23666762

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a(CHEBI:"methylene blue") increases deg(p(HGNC:MARK4)) View Subject | View Object

In 293T culture, MB decreased MARK4-mediated Tau phosphorylation in a dose dependent manner. MB down-regulates MARK4 protein level through ubiquitin-proteasome pathway and inhibition of MARK4 kinase activity in vitro. PubMed:23666762

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a(GO:"dendritic spine") 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

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Annotations
Uberon
hippocampal formation

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

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Annotations
Uberon
hippocampal formation

p(HBP:"CagA peptide") decreases act(p(HGNC:MARK4), ma(kin)) View Subject | View Object

In cells, a CagA peptide inhibited tau phosphorylation at Ser²6² mediated by MARK4 but not other MARK isoforms. A strong and significant elevation of MARK4 expression and MARK4-tau interactions in AD brains correlated with the Braak stages of the disease. PubMed:23666762

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p(HBP:PrPSc) negativeCorrelation p(HGNC:MARK4) View Subject | View Object

MARK4 was extremely decreased in the brain regions with a mass of PrPSc in a G114V gCJD patient, but was clearly observable in the regions with a minimum amount of PrPSc or without detectable PrPSc in a D178N FFI patient. PubMed:22692785

act(p(RGD:Dlg4)) 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

p(RGD:Gria1) 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

path(MESH:"Alzheimer Disease") positiveCorrelation p(HGNC:MARK4) View Subject | View Object

In cells, a CagA peptide inhibited tau phosphorylation at Ser²6² mediated by MARK4 but not other MARK isoforms. A strong and significant elevation of MARK4 expression and MARK4-tau interactions in AD brains correlated with the Braak stages of the disease. PubMed:23666762

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Out-Edges 8

p(HGNC:MARK4) negativeCorrelation p(HBP:PrPSc) View Subject | View Object

MARK4 was extremely decreased in the brain regions with a mass of PrPSc in a G114V gCJD patient, but was clearly observable in the regions with a minimum amount of PrPSc or without detectable PrPSc in a D178N FFI patient. PubMed:22692785

p(HGNC:MARK4) positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

In cells, a CagA peptide inhibited tau phosphorylation at Ser²6² mediated by MARK4 but not other MARK isoforms. A strong and significant elevation of MARK4 expression and MARK4-tau interactions in AD brains correlated with the Braak stages of the disease. PubMed:23666762

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p(HGNC:MARK4) increases a(HBP:"Tau epitope, 12E8") 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(HGNC:MARK4) negativeCorrelation act(p(RGD:Dlg4)) 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(HGNC:MARK4) negativeCorrelation p(RGD:Gria1) 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(HGNC:MARK4) negativeCorrelation a(GO:"dendritic spine") 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(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

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