INT263746

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Context Info
Confidence 0.27
First Reported 2009
Last Reported 2009
Negated 0
Speculated 2
Reported most in Body
Documents 1
Total Number 14
Disease Relevance 0
Pain Relevance 0.48

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

plasma membrane (Dlg4, Neto1) structural molecule activity (Dlg4) protein complex assembly (Dlg4)
cytoplasm (Dlg4)
Anatomy Link Frequency
synapses 3
tail 1
Dlg4 (Mus musculus)
Neto1 (Mus musculus)
Pain Link Frequency Relevance Heat
Glutamate receptor 28 97.92 Very High Very High Very High
long-term potentiation 364 97.32 Very High Very High Very High
Hippocampus 168 88.00 High High
addiction 14 28.76 Quite Low
cerebral cortex 14 12.48 Low Low
Central nervous system 42 9.60 Low Low
nMDA receptor 126 5.00 Very Low Very Low Very Low
Pyramidal cell 56 5.00 Very Low Very Low Very Low
Neurotransmitter 42 5.00 Very Low Very Low Very Low
Eae 28 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Sprains And Strains 14 32.08 Quite Low
Convulsion 28 14.04 Low Low
Cognitive Disorder 112 5.00 Very Low Very Low Very Low
Congenital Anomalies 84 5.00 Very Low Very Low Very Low
Helminth Infection 14 5.00 Very Low Very Low Very Low
Influenza Virus Infection 14 5.00 Very Low Very Low Very Low
Contagious Ecthyma 14 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These results indicate that the binding of Neto1 to PSD-95 was not required for Neto1 to interact with the NMDAR, and that Neto1 interacts with NMDARs through a PSD-95-independent mechanism.


PSD-95 Binding (binding) of Neto1
1) Confidence 0.27 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.03
We have shown that Neto1 interacts with NMDARs through the extracellular domain of their NR2 subunits, as well as intracellularly through PSD-95.
PSD-95 Binding (interacts) of Neto1
2) Confidence 0.27 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.15
The Neto1 cytoplasmic domain bound most strongly to PDZ3 of PSD-95, binding that was completely dependent on the C-terminal TRV of Neto1, in both the two-hybrid system (Figure S2) and in HEK293 cells (Figure 2F, lane 2).
PSD-95 Binding (bound) of Neto1
3) Confidence 0.21 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.05
To determine whether the association of Neto1 with NMDARs was entirely dependent upon the binding of its C-terminal PDZ ligand to PSD-95, we examined the binding of PSD-95 to an hemagglutinin (HA)-tagged Neto1 protein lacking the C-terminal 20 amino acids (Neto1-?
PSD-95 Binding (binding) of Neto1
4) Confidence 0.20 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.05
To determine whether the association of Neto1 with NMDARs was entirely dependent upon the binding of its C-terminal PDZ ligand to PSD-95, we examined the binding of PSD-95 to an hemagglutinin (HA)-tagged Neto1 protein lacking the C-terminal 20 amino acids (Neto1-?
PSD-95 Spec (examined) Binding (binding) of Neto1
5) Confidence 0.20 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.05
As predicted both by the interaction between PSD-95 and the NR2 subunits of the NMDAR [28], and by the binding of Neto1 to PSD-95 described above, we found that Neto1 was co-immunoprecipitated by anti-NR1 antibodies from lysates of cells co-expressing Neto1, PSD-95, NR1, and NR2B (Figure 4A, lane 1).
PSD-95 Binding (binding) of Neto1
6) Confidence 0.20 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.04
To determine whether the association of Neto1 with NMDARs was entirely dependent upon the binding of its C-terminal PDZ ligand to PSD-95, we examined the binding of PSD-95 to an hemagglutinin (HA)-tagged Neto1 protein lacking the C-terminal 20 amino acids (Neto1-?
PSD-95 Spec (examined) Binding (binding) of Neto1
7) Confidence 0.20 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.05
The yeast two-hybrid system was initially used to determine whether the cytoplasmic tail of Neto1 could interact with PSD-95 and the related proteins PSD-93, SAP-102, and SAP-97.
PSD-95 Binding (interact) of Neto1 in tail
8) Confidence 0.20 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
Altogether, these findings indicate that Neto1 associates with PSD-95 in brain synapses through the binding of its C-terminal tripeptide with the PDZ domains of PSD-95.


PSD-95 Binding (binding) of Neto1 in synapses
9) Confidence 0.20 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
To identify the region of Neto1 that mediates the PSD-95-independent association between Neto1 and NMDARs, we examined the ability of a series of C-terminally deleted Neto1 proteins to co-immunoprecipitate with NMDARs from HEK293 cell lysates.
PSD-95-independent Binding (association) of Neto1
10) Confidence 0.18 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.03
These results indicate that the binding of Neto1 to PSD-95 was not required for Neto1 to interact with the NMDAR, and that Neto1 interacts with NMDARs through a PSD-95-independent mechanism.


PSD-95-independent Binding (interacts) of Neto1
11) Confidence 0.18 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.03
Altogether, these findings indicate that Neto1 associates with PSD-95 in brain synapses through the binding of its C-terminal tripeptide with the PDZ domains of PSD-95.


PSD-95 Binding (binding) of Neto1 in synapses
12) Confidence 0.18 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
Altogether, these findings indicate that Neto1 associates with PSD-95 in brain synapses through the binding of its C-terminal tripeptide with the PDZ domains of PSD-95.


PSD-95 Binding (associates) of Neto1 in synapses
13) Confidence 0.18 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
Moreover, the Neto1 cytoplasmic domain bound to a truncated PSD-95 polypeptide (PDZ1–3) containing only the three PDZ domains (Figure 2F, lane 3).
truncated PSD-95 polypeptide Binding (bound) of Neto1
14) Confidence 0.18 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0

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