INT238632

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Context Info
Confidence 0.44
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 10
Disease Relevance 0.78
Pain Relevance 0.27

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

protein complex (EPB41, Cask) cytoplasm (EPB41, Cask) nucleus (EPB41, Cask)
plasma membrane (EPB41, Cask) Golgi apparatus (EPB41) intracellular (Cask)
Anatomy Link Frequency
spine 2
synapse 1
EPB41 (Homo sapiens)
Cask (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Calcium channel 20 78.48 Quite High
Glutamate receptor 30 74.28 Quite High
Neurotransmitter 10 43.16 Quite Low
cerebral cortex 30 40.16 Quite Low
midbrain 20 38.56 Quite Low
tetrodotoxin 100 15.68 Low Low
GABAergic 10 11.20 Low Low
Disease Link Frequency Relevance Heat
Adhesions 60 95.44 Very High Very High Very High
Aids-related Complex 10 92.20 High High
Targeted Disruption 60 38.16 Quite Low
Cleft Palate 20 5.00 Very Low Very Low Very Low
Myelodysplastic Syndromes 10 5.00 Very Low Very Low Very Low
Apoptosis 10 5.00 Very Low Very Low Very Low
Stroke 10 5.00 Very Low Very Low Very Low
Cytomegalovirus Infection 10 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
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.
protein 4.1 Binding (interaction) of CASK
1) Confidence 0.44 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.15 Pain Relevance 0.07
Because protein 4.1 interacts with spectrin and promotes the interaction between spectrin and filamentous actin, reduction of the interaction between CASK and protein 4.1 by SUMOylation would be expected to attenuate the association between CASK and filamentous actin.
protein 4.1 Binding (interaction) of CASK
2) Confidence 0.38 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
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.
protein 4.1 Binding (interaction) of CASK
3) Confidence 0.38 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
Because CASK also interacts with protein 4.1 (Cohen et al., 1998; Biederer and Sudhof, 2001) and because the function of protein 4.1 is to bind spectrin, a postsynaptic density protein required for synapse formation (Sytnyk et al., 2006), and to promote the interaction between spectrin and actin cytoskeleton (for reviews see Hoover and Bryant, 2000; Bretscher et al., 2002), it is reasonable to speculate that the role of CASK in spinogenesis is to link the plasma membrane proteins, such as syndecan-2 and SynCAM, to the actin cytoskeleton.
protein 4.1 Binding (interacts) of CASK in synapse
4) Confidence 0.38 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
We also identified SUMOylation as a posttranslational modification of CASK that regulates the interaction between CASK and protein 4.1 and, thus, modulates spinogenesis.
protein 4.1 Binding (interaction) of CASK
5) Confidence 0.38 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0.07
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.
protein 4.1 Binding (interaction) of CASK
6) Confidence 0.38 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.15 Pain Relevance 0.07
SUMOylation of CASK modulates the interaction between CASK and protein 4.1 and contributes to spinogenesis.


protein 4.1 Binding (interaction) of CASK
7) Confidence 0.38 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.23 Pain Relevance 0
S3), which may be caused by either impairment of spine formation by C-SUMO1-CASK or an attenuation of the interaction between C-SUMO1-CASK and protein 4.1.


protein 4.1 Binding (interaction) of SUMO1-CASK in spine
8) Confidence 0.33 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0.03
S3), which may be caused by either impairment of spine formation by C-SUMO1-CASK or an attenuation of the interaction between C-SUMO1-CASK and protein 4.1.


protein 4.1 Binding (interaction) of SUMO1-CASK in spine
9) Confidence 0.33 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0.03
SUMOylation of CASK modulates the interaction between CASK and protein 4.1 and contributes to spinogenesis.


protein 4.1 Binding (interaction) of CASK
10) Confidence 0.33 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.24 Pain Relevance 0

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