INT90545

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Context Info
Confidence 0.11
First Reported 2000
Last Reported 2010
Negated 3
Speculated 0
Reported most in Body
Documents 53
Total Number 53
Disease Relevance 12.09
Pain Relevance 6.81

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

extracellular region (Siglec1) cell adhesion (Siglec1) plasma membrane (Siglec1)
Anatomy Link Frequency
fibroblasts 2
neuronal 1
tail 1
brain 1
Siglec1 (Mus musculus)
Siglec1 - S553P (1)
Pain Link Frequency Relevance Heat
Catecholamine 180 99.32 Very High Very High Very High
bradykinin 150 99.22 Very High Very High Very High
Inflammation 46 98.34 Very High Very High Very High
b2 receptor 2 97.92 Very High Very High Very High
dorsal root ganglion 1 97.60 Very High Very High Very High
Dopamine 747 96.96 Very High Very High Very High
agonist 27 95.68 Very High Very High Very High
Enkephalin 6 95.52 Very High Very High Very High
opioid receptor 12 94.08 High High
Eae 14 92.24 High High
Disease Link Frequency Relevance Heat
Parkinson's Disease 660 99.58 Very High Very High Very High
Disease 656 99.24 Very High Very High Very High
Targeted Disruption 469 98.92 Very High Very High Very High
Stress 293 98.48 Very High Very High Very High
INFLAMMATION 47 98.34 Very High Very High Very High
Ganglion Cysts 1 97.60 Very High Very High Very High
Down Syndrome 32 96.72 Very High Very High Very High
Death 135 96.60 Very High Very High Very High
Apoptosis 181 94.84 High High
Aging 92 93.16 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Phosphorylation of GluR1 at Ser 831 and Ser 845 sites is important for GluR1 trafficking [50].
Phosphorylation (Phosphorylation) of Ser
1) Confidence 0.11 Published 2010 Journal Mol Brain Section Body Doc Link PMC2822766 Disease Relevance 0.15 Pain Relevance 0.21
Importantly, Ser(P)-129 is not dephosphorylated by PP2A (72), a finding that we have also reconfirmed (Fig. 7B).
Neg (not) Phosphorylation (dephosphorylated) of Ser
2) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.35 Pain Relevance 0
Together these data imply that when a-Syn is dephosphorylated on Ser-129, the molecule becomes a more potent regulator of TH and PP2A than when Ser-129 on a-Syn is phosphorylated.
Phosphorylation (dephosphorylated) of Ser
3) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0.08
Although that study did not measure the effect of native a-Syn phosphorylation, their work clearly supports our findings that TH inhibition is attenuated by a-Syn Ser-129 phosphorylation (Fig. 7C), which likely led to the measurable increase in TH-Ser(P)-40 and dopamine noted in their S129D cells.
Phosphorylation (phosphorylation) of Ser associated with dopamine
4) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.14 Pain Relevance 0.05
Here we demonstrate that a-Syn significantly inhibited TH activity in vitro and in vivo and that phosphorylation of a-Syn serine 129 (Ser-129) modulated this effect.
Phosphorylation (phosphorylation) of Ser
5) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Abstract Doc Link PMC2878529 Disease Relevance 0.15 Pain Relevance 0.13
We confirmed equivalent a-Syn in each reaction and verified Ser-129 phosphorylation by immunoblots using an antibody specific for a-Syn Ser(P)-129 (Fig. 7A).
Phosphorylation (phosphorylation) of Ser
6) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0.03
In MN9D cells, a-Syn overexpression reduced TH serine 19 phosphorylation (Ser(P)-19).
Phosphorylation (phosphorylation) of Ser
7) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Abstract Doc Link PMC2878529 Disease Relevance 0.15 Pain Relevance 0.13
Collectively our findings provide compelling support for physiological regulation of PP2A and TH by a-Syn, with a-Syn Ser-129 phosphorylation attenuating the effects.
Phosphorylation (phosphorylation) of Ser
8) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.36 Pain Relevance 0
Because the above experiments were performed using S129A dephosphorylation mutant, this series of experiments was performed to directly compare unphosphorylated a-Syn to a-Syn phosphorylated on Ser-129 for potential differences in PP2A activity.
Phosphorylation (phosphorylated) of Ser
9) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0.03
Together these data imply that when a-Syn is dephosphorylated on Ser-129, the molecule becomes a more potent regulator of TH and PP2A than when Ser-129 on a-Syn is phosphorylated.
Phosphorylation (phosphorylated) of Ser
10) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0.08
PP2A does not dephosphorylate a-Syn Ser-129 (72), and we confirmed this in our experiments where background signal-only was noted for both PLK2+- and PLK2-a-Syn-treated samples (Fig. 7B, left).
Neg (not) Phosphorylation (dephosphorylate) of Ser
11) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0
Phosphorylation of a-Syn Ser-129 in a Cell-free System Attenuates a-Syn Modulatory Effects on PP2A and TH
Phosphorylation (Phosphorylation) of Ser
12) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0.07
Therefore, this study was undertaken to 1) further elucidate the molecular mechanisms underlying the effects of a-Syn on TH, especially Ser-19 phosphorylation, which represents a key step in 14-3-3-mediated-TH activation, 2) determine the in vivo significance of a-Syn in TH regulation in transgenic overexpressing and null mice, and 3) assess if a-Syn Ser-129 phosphorylation affects a-Syn function toward PP2A or TH.
Phosphorylation (phosphorylation) of Ser-19 associated with targeted disruption
13) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.57 Pain Relevance 0
To directly measure the impact of Ser-129 phosphorylation of a-Syn on PP2A and TH, we used recombinant proteins and cell-free assays.


Phosphorylation (phosphorylation) of Ser
14) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0.07
Although Ser(P)-129 a-Syn is strongly implicated in PD pathogenesis, no one has evaluated if Ser-129 phosphorylation on a-Syn affects a-Syn function.
Phosphorylation (phosphorylation) of Ser associated with parkinson's disease
15) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.10 Pain Relevance 0
Immunoblots show Ser(P)-129 in all cells with higher levels noted for cells that overexpressed a-Syn, confirming Ser-129 phosphorylation in MN9D cells at base line (Fig. 5A).
Phosphorylation (phosphorylation) of Ser
16) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.08 Pain Relevance 0
We confirmed equivalent a-Syn in each reaction and verified Ser-129 phosphorylation by immunoblots using an antibody specific for a-Syn Ser(P)-129 (Fig. 7A).
Phosphorylation (phosphorylation) of Ser
17) Confidence 0.10 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0.03
Importantly, Ser(P)-129 is not dephosphorylated by PP2A (72), a finding that we verified (Fig. 7B). a-Syn can be phosphorylated by at least three kinases, including casein kinase 2 (72, 96–99), G-protein-coupled receptor kinase 5 (100), and Polo-like kinases, especially PLK2, which exclusively phosphorylates Ser-129 (101).
Neg (not) Phosphorylation (dephosphorylated) of Ser
18) Confidence 0.08 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.54 Pain Relevance 0.16
These data provide the first evidence that native phosphorylation of a-Syn Ser-129 attenuates a-Syn ability to stimulate PP2A activity.
Phosphorylation (phosphorylation) of Ser
19) Confidence 0.08 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0.04
a-Syn mutations (A30P, A53T, or E46K) (32–34) and multiplications (35, 36) induce rare forms of familial Parkinson disease (PD), and a-Syn is a major protein in Lewy bodies, the intraneuronal protein aggregates characteristic of PD (37). a-Syn that is phosphorylated at serine 129 (Ser(P)-129) is plentiful in Lewy bodies (38, 39), yet no one knows how a-Syn Ser-129 phosphorylation affects a-Syn function.
Phosphorylation (phosphorylated) of Ser associated with parkinson's disease
20) Confidence 0.08 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.49 Pain Relevance 0.09

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