INT221557

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.76
First Reported 2007
Last Reported 2007
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 21
Disease Relevance 2.49
Pain Relevance 0.76

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

lipid binding (Fes) Golgi apparatus (Fes) plasma membrane (Fes)
cytoskeleton (Fes) kinase activity (Fes) cytoplasm (Fes)
Anatomy Link Frequency
upper 4
brains 2
mast cells 1
Fes (Mus musculus)
Pain Link Frequency Relevance Heat
dorsal root ganglion 777 94.24 High High
nociceptor 21 76.44 Quite High
withdrawal 21 5.00 Very Low Very Low Very Low
Root ganglion neuron 21 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Shock 462 98.44 Very High Very High Very High
Ganglion Cysts 798 94.24 High High
Sprains And Strains 42 86.20 High High
Adhesions 21 85.20 High High
Apoptosis 63 5.00 Very Low Very Low Very Low
Targeted Disruption 63 5.00 Very Low Very Low Very Low
Death 21 5.00 Very Low Very Low Very Low
Wallerian Degeneration 21 5.00 Very Low Very Low Very Low
Urological Neuroanatomy 21 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Fps was previously identified in a complex with CRMP2 and CRAM in neonatal rat brains; and in co-transfection studies, Fps was shown to phosphorylate all four CRMPs [20].
Phosphorylation (phosphorylate) of Fps in brains
1) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0 Pain Relevance 0
Compared to wt, the Fps plus Fer kinase autophosphorylation was only slightly reduced in fps-/- lysates, substantially reduced in ferDR/DR, and abolished in fpsKR/KR/ferDR/DR lysates (Fig. 3A, upper).
Phosphorylation (autophosphorylation) of Fps in upper
2) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.09 Pain Relevance 0
These assays were performed both in the presence and absence of ATP to control for the relatively low levels of in vivo tyrosine phosphorylation of Fps or Fer, which was not detectable under these conditions.
Phosphorylation (phosphorylation) of Fps
3) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.12 Pain Relevance 0.06
PlexinA1 inhibits the autophosphorylation activities of Fps and Fer
Phosphorylation (autophosphorylation) of Fps
4) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.17 Pain Relevance 0.08
In Cos-7 transfection studies, Mitsui and colleagues showed a Fps-mediated phosphorylation of PlexinA1 [20].
Phosphorylation (phosphorylation) of Fps
5) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.16 Pain Relevance 0.16
Since tubulin is the major structural component of microtubules, the potential of Fer and Fps to phosphorylate tubulin in vivo, and the role that might play in microtubule dynamics will certainly merit further study.
Phosphorylation (phosphorylate) of Fps
6) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.35 Pain Relevance 0.07
Interestingly, the in vivo tyrosine phosphorylation status of both Fps and Fer were significantly reduced by co-expression with CRMP2 (Fig. 4A, upper).
Phosphorylation (phosphorylation) of Fps in upper
7) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0 Pain Relevance 0
However, co-expression of PlexinA1 correlated with reduced autophosphorylation of both Fps and Fer (Fig. 4A, upper).
Phosphorylation (autophosphorylation) of Fps in upper
8) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.13 Pain Relevance 0.06
Although we were unable to detect physical interactions between PlexinA1 nor CRMP2 with either kinase, we observed that both PlexinA1 and CRMP2 inhibited the autophosphorylation activities of Fps and Fer.
Phosphorylation (autophosphorylation) of Fps
9) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0 Pain Relevance 0
Given the apparent ability of PlexinA1 and CRMP2 to inhibit Fps and Fer autophosphorylation, we conclude that some interaction must have been occurring, but it failed to survive our immunoprecipitation protocol.
Phosphorylation (autophosphorylation) of Fps
10) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0 Pain Relevance 0
PlexinA1 association with and phosphorylation by Fps or Fer were first examined in co-transfection studies.
Phosphorylation (phosphorylation) of Fps
11) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.18 Pain Relevance 0.09
A similar inhibition of both Fps and Fer autophosphorylation was observed in vitro when the purified GST-PlexinA1 protein was added as an exogenous substrate to anti-Fps/Fer immunoprecipitates from neonatal wt, fpsKR/KR, ferDR/DR or fpsKR/KR/ferDR/DR mouse brains (Fig. 4B, upper).
Phosphorylation (autophosphorylation) of Fps in upper
12) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.05 Pain Relevance 0.03
Purified Fps was also reported to phosphorylate tubulin and promote its polymerization in vitro; and biochemical association between Fps and soluble tubulin was dependent upon the Fps FCH domain [22].
Phosphorylation (phosphorylate) of Fps
13) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0 Pain Relevance 0
Furthermore, like PlexinA1, CRMP2 inhibited the in vivo autophosphorylation activity of Fps and Fer.
Phosphorylation (autophosphorylation) of Fps
14) Confidence 0.76 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.19 Pain Relevance 0.06
A comparison of the relative amounts of Fps and Fer (Fig. 5A, lower) with the degree of CRMP2 tyrosine phosphorylation suggests that CRMP2 was a much better substrate for Fer than it was for Fps under these conditions.
Phosphorylation (phosphorylation) of Fps
15) Confidence 0.59 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0 Pain Relevance 0
Collectively, these results show that Fer is expressed at substantially higher levels than Fps in whole neonatal mouse brain and DRGs; and furthermore, that Fer, but not Fps, is detectably tyrosine phosphorylated in vivo, and is therefore presumably active in neonatal brains.


Phosphorylation (phosphorylated) of Fps in brains
16) Confidence 0.59 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0 Pain Relevance 0
There is also evidence that Fyn might regulate Fps, and possibly Fer, as Fyn has been shown to phosphorylate a kinase-defective mutant form of Fps in Sf-9 cells [45], Fer and Fyn cooperate in actin depolymerization-induced cortactin phosphorylation [26], and the Fyn-related Lyn kinase regulates Fer phosphorylation in mast cells downstream of the IgE receptor engagement [46].
Phosphorylation (phosphorylate) of Fps in mast cells
17) Confidence 0.59 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.15 Pain Relevance 0
In Cos-7 cell co-transfection studies, Fps promoted the phosphorylation of both CRMP/CRAM proteins and the Semaphorin receptor signal transducing subunit PlexinA1; and Sema3A promoted the PlexinA1 association with, and phosphorylation by Fps [20].
Phosphorylation (phosphorylation) of Fps
18) Confidence 0.59 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.37 Pain Relevance 0.04
It will be important to map the Fps and Fer tyrosine phosphorylation sites in CRMP2 and determine if these phosphorylations affect its ability to bind to tubulin or microtubule regulator proteins.
Phosphorylation (phosphorylation) of Fps
19) Confidence 0.59 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.40 Pain Relevance 0.08
Similarly, it is possible that the VSV epitope tag on the recombinant PlexinA1 used in our study was permissive of associations that compromised kinase autophosphorylation, but precluded PlexinA1 phosphorylation, and subsequent high affinity associations with Fps or Fer.
Phosphorylation (phosphorylation) of Fps
20) Confidence 0.59 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.05 Pain Relevance 0.03

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox