INT238602

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Context Info
Confidence 0.40
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 17
Disease Relevance 0.90
Pain Relevance 0.63

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

cytosol (Cask) nucleolus (Cask) plasma membrane (Cask)
nucleus (Cask) intracellular (Cask) protein complex assembly (Cask)
Anatomy Link Frequency
neurons 2
spines 2
tail 2
Cask (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Calcium channel 34 99.66 Very High Very High Very High
Neurotransmitter 17 96.56 Very High Very High Very High
tetrodotoxin 170 90.08 High High
Glutamate receptor 51 70.32 Quite High
cerebral cortex 51 41.40 Quite Low
GABAergic 17 37.28 Quite Low
midbrain 34 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cleft Palate 34 94.72 High High
Adhesions 102 93.92 High High
Aids-related Complex 17 88.24 High High
Targeted Disruption 102 86.40 High High
Apoptosis 17 37.16 Quite Low
Myelodysplastic Syndromes 17 5.00 Very Low Very Low Very Low
Stroke 17 5.00 Very Low Very Low Very Low
Cytomegalovirus Infection 17 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Because the protein 4.1–binding site covers only around 10 amino acid residues, it was inconvenient to simply express the protein 4.1–binding site alone to interrupt the interaction between endogenous CASK and protein 4.1.
CASK Binding (interaction) of
1) Confidence 0.40 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
In addition to spinogenesis, CASK also acts presynaptically to regulate synaptogenesis through a different mechanism: CDK5 phosphorylates residues S51 and S395 of CASK proteins, which enhances the interaction between CASK and N-type calcium channels but impairs the interaction between CASK and liprin-?
CASK Binding (interaction) of associated with calcium channel
2) Confidence 0.40 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.06 Pain Relevance 0.09
Two dominant-negative mutants that interrupt the interactions between endogenous CASK and the PDZ-binding molecules, the CASK PDZ domain alone (PDZ) and the cytoplasmic tail of syndecan-2 (synd-2C), were cotransfected with GFP into cultured hippocampal neurons.
CASK Binding (interactions) of in tail
3) Confidence 0.40 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
In addition to spinogenesis, CASK also acts presynaptically to regulate synaptogenesis through a different mechanism: CDK5 phosphorylates residues S51 and S395 of CASK proteins, which enhances the interaction between CASK and N-type calcium channels but impairs the interaction between CASK and liprin-?
CASK Binding (interaction) of associated with calcium channel
4) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.06 Pain Relevance 0.10
CASK also interacts with liprin-?
CASK Binding (interacts) of
5) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0.05
We then wondered whether the CASK protein 4.1–binding site is also required for spinogenesis.
CASK Binding (binding) of
6) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
Via the interactions with its binding partners, CASK plays multiple roles in neurons.
CASK Binding (interactions) of in neurons
7) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0.03
Because CASK and protein 4.1 are widely expressed in different tissues, SUMOylation of CASK may also regulate the interaction between CASK and protein 4.1 in nonneuronal cells.
CASK Binding (interaction) of
8) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.18 Pain Relevance 0
SUMOylation of CASK modulates the interaction between CASK and protein 4.1, which may therefore down-regulate the association between CASK and the actin cytoskeleton.
CASK Binding (association) of
9) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.15 Pain Relevance 0.07
Because SUMOylation usually modifies target protein–protein interaction, distribution, or activity, we wondered whether CASK is SUMOylated and whether CASK SUMOylation affects the interaction between CASK and protein 4.1 and thus regulates the function of CASK in spinogenesis.
CASK Binding (interaction) of
10) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
Because protein 4.1 binds spectrin, an abundant component at the postsynaptic density, and thus promotes the interaction between spectrin and filamentous actin (for reviews see Hoover and Bryant, 2000;Bretscher et al., 2002), CASK may act as a linker between transmembrane proteins and the actin cytoskeleton and, therefore, stabilize dendritic spines.
CASK Binding (binds) of in spines
11) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.14 Pain Relevance 0
Two dominant-negative mutants that interrupt the interactions between endogenous CASK and the PDZ-binding molecules, the CASK PDZ domain alone (PDZ) and the cytoplasmic tail of syndecan-2 (synd-2C), were cotransfected with GFP into cultured hippocampal neurons.
CASK Binding (interactions) of in tail
12) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
Because SUMOylation of CASK regulates the interaction between CASK and protein 4.1 and because the interaction with protein 4.1 is required for CASK function in spinogenesis, we then investigated whether CASK SUMOylation modulates spine formation.
CASK Binding (interaction) of in spine
13) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0.30
Conjugation of small ubiquitin-like modifier 1 (SUMO1) to CASK reduces the interaction between CASK and protein 4.1.
CASK Binding (interaction) of
14) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Abstract Doc Link PMC2447900 Disease Relevance 0.16 Pain Relevance 0
CASK SUMOylation reduces the interaction between CASK and protein 4.1
CASK Binding (interaction) of
15) Confidence 0.34 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
Echoing recent exciting studies showing the role of SUMOylation in neurons (Martin et al., 2007; Shalizi et al., 2006, 2007; van Niekerk et al., 2007), we found that CASK is SUMOylated in neurons and that SUMOylation affects the interaction between CASK and protein 4.1 and alters spine morphology.


CASK Binding (interaction) of in neurons
16) Confidence 0.34 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.15 Pain Relevance 0
We then wondered whether CASK SUMOylation regulates the interaction between CASK and protein 4.1.
CASK Binding (interaction) of
17) Confidence 0.34 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0

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