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Appears in Networks 6

In-Edges 38

a(MESH:Mitochondria) association p(FPLX:PPP2) View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

complex(p(FPLX:PPP2), p(HGNC:MAPT)) positiveCorrelation act(p(FPLX:PPP2)) View Subject | View Object

Notably, methylation of PP2A catalytic C subunit on the Leu- 309 residue by leucine carboxyl methyltransferase 1 (LCMT1) promotes the biogenesis and stabilization of PP2A/B enzymes (20). We have shown that decreased LCMT1 activity and/or expression levels correlate with down-regulation of PP2A methylation and PP2A/B expression levels and with concomitant accumulation of phospho-Tau in AD-affected brain regions (21), in cultured N2a neuroblastoma cells and in vivo PubMed:23943618

Appears in Networks:
Annotations
Disease Ontology (DO)
Alzheimer's disease

p(HGNC:PPP2CA, pmod(Me, Leu, 309)) increases act(p(FPLX:PPP2)) View Subject | View Object

Notably, methylation of PP2A catalytic C subunit on the Leu- 309 residue by leucine carboxyl methyltransferase 1 (LCMT1) promotes the biogenesis and stabilization of PP2A/B enzymes (20). We have shown that decreased LCMT1 activity and/or expression levels correlate with down-regulation of PP2A methylation and PP2A/B expression levels and with concomitant accumulation of phospho-Tau in AD-affected brain regions (21), in cultured N2a neuroblastoma cells and in vivo PubMed:23943618

Appears in Networks:
Annotations
Disease Ontology (DO)
Alzheimer's disease

p(HGNC:UNC5B) positiveCorrelation act(p(FPLX:PPP2), ma(kin)) View Subject | View Object

Overexpression of UNC5B induces neuronal death by activating death-associated protein kinase (DAPK1) (19) via protein phosphatase 2A-mediated dephosphorylation of DAPK1 (20). PubMed:27068745

Appears in Networks:

a(CHEBI:Tautomycin) decreases act(p(FPLX:PPP2)) View Subject | View Object

Potent tumor promoter, Okadaic acid (a microbial toxin), inhibits the enzymatic activity of PP2Ac and thereby has facilitated various studies to understand the functional aspects of PP2A and other phosphatases [12]. Other than Okadaic acid, calyculin A, microcystin, cantharidin, nodularm, fostriecin and tautomycin are able to inhibit PP2A activity at different IC50 values [48]. PubMed:23454242

a(CHEBI:cantharidin) decreases act(p(FPLX:PPP2)) View Subject | View Object

Potent tumor promoter, Okadaic acid (a microbial toxin), inhibits the enzymatic activity of PP2Ac and thereby has facilitated various studies to understand the functional aspects of PP2A and other phosphatases [12]. Other than Okadaic acid, calyculin A, microcystin, cantharidin, nodularm, fostriecin and tautomycin are able to inhibit PP2A activity at different IC50 values [48]. PubMed:23454242

a(CHEBI:microcystin) decreases act(p(FPLX:PPP2)) View Subject | View Object

Potent tumor promoter, Okadaic acid (a microbial toxin), inhibits the enzymatic activity of PP2Ac and thereby has facilitated various studies to understand the functional aspects of PP2A and other phosphatases [12]. Other than Okadaic acid, calyculin A, microcystin, cantharidin, nodularm, fostriecin and tautomycin are able to inhibit PP2A activity at different IC50 values [48]. PubMed:23454242

a(PUBCHEM:4162) decreases act(p(FPLX:PPP2)) View Subject | View Object

Potent tumor promoter, Okadaic acid (a microbial toxin), inhibits the enzymatic activity of PP2Ac and thereby has facilitated various studies to understand the functional aspects of PP2A and other phosphatases [12]. Other than Okadaic acid, calyculin A, microcystin, cantharidin, nodularm, fostriecin and tautomycin are able to inhibit PP2A activity at different IC50 values [48]. PubMed:23454242

a(PUBCHEM:5311365) decreases act(p(FPLX:PPP2)) View Subject | View Object

Potent tumor promoter, Okadaic acid (a microbial toxin), inhibits the enzymatic activity of PP2Ac and thereby has facilitated various studies to understand the functional aspects of PP2A and other phosphatases [12]. Other than Okadaic acid, calyculin A, microcystin, cantharidin, nodularm, fostriecin and tautomycin are able to inhibit PP2A activity at different IC50 values [48]. PubMed:23454242

a(PUBCHEM:6913994) decreases act(p(FPLX:PPP2)) View Subject | View Object

Potent tumor promoter, Okadaic acid (a microbial toxin), inhibits the enzymatic activity of PP2Ac and thereby has facilitated various studies to understand the functional aspects of PP2A and other phosphatases [12]. Other than Okadaic acid, calyculin A, microcystin, cantharidin, nodularm, fostriecin and tautomycin are able to inhibit PP2A activity at different IC50 values [48]. PubMed:23454242

a(PUBCHEM:71361092) decreases act(p(FPLX:PPP2)) View Subject | View Object

In addition to microbial toxin, viral protein SV40 (potent oncogene) also inactivates PP2A action by binding to the AC dimer and displacing the PR56 (PP2A-B’ γ ) subunit [35]. PubMed:23454242

p(FPLX:PPP2, pmod(Me)) association act(p(FPLX:PPP2)) View Subject | View Object

Methylation [52] and phosphorylation [53] are two major modifications that have been shown to modulate PP2A catalytic efficiency. PubMed:23454242

p(FPLX:PPP2, pmod(Me, Leu, 309)) increases act(p(FPLX:PPP2)) View Subject | View Object

The addition of a methyl group by LCMT1 at L309 enhances the binding affinity of the core dimer (A&C subunit) toward distinct regulatory subunits and provides specific activity to the holoenzyme [56]. PubMed:23454242

p(FPLX:PPP2, pmod(Ph)) association act(p(FPLX:PPP2)) View Subject | View Object

Methylation [52] and phosphorylation [53] are two major modifications that have been shown to modulate PP2A catalytic efficiency. PubMed:23454242

p(FPLX:PPP2, pmod(Ph, Tyr, 307)) decreases act(p(FPLX:PPP2)) View Subject | View Object

Phosphorylation of Y307 by receptor associated tyrosine kinases effectively decreases the PP2A activity by inhibiting the interaction of PP2Ac with the PP2A-PR55/PR61 subunit [54]. PubMed:23454242

path(MESH:"Alzheimer Disease") decreases act(p(FPLX:PPP2)) View Subject | View Object

In Alzheimer's disease, inhibition of PP2A activity by SET leads to hyper phosphorylation of the Tau protein [47]. PubMed:23454242

path(MESH:"Cell Transformation, Neoplastic") association p(FPLX:PPP2) View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

path(MESH:Neoplasms) association p(FPLX:PPP2) View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

path(MESH:Neoplasms) negativeCorrelation act(p(FPLX:PPP2)) View Subject | View Object

PP2A is considered as a tumor suppressor and is thought to be functionally inactivated in cancer. PubMed:23454242

a(MESH:Cytosol) association p(FPLX:PPP2) View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

a(CHEBI:"okadaic acid") decreases act(p(FPLX:PPP2)) View Subject | View Object

Similar findings have been observed in metabolically active rat brain slices, where a selective inhibition of PP2A with OA results in an aberrant phosphorylation of tau at the same residues seen in AD brains at serines (Ser) 198, 199, 202, 396, 404, 422 and 262 [11, 47, 48]. PubMed:22299660

a(HBP:"paired helical filaments") negativeCorrelation act(p(FPLX:PPP2)) View Subject | View Object

Studies in transgenic mice and in cell cultures have shown a connection between PP2A loss of function and tau hyper-phosphorylation and aggregation into PHF. PubMed:22299660

a(MESH:"Cell Membrane") association p(FPLX:PPP2) View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

a(MESH:"Cell Nucleus") association p(FPLX:PPP2) View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

a(MESH:Cytoskeleton) association p(FPLX:PPP2) View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

p(FPLX:PPP2C, pmod(Ph, Tyr, 307)) increases act(p(FPLX:PPP2)) View Subject | View Object

The other important post-translational modi- fication is phosphorylation of PP2A C at Tyr307 which in- hibits PP2A activity [74-76]. PubMed:22299660

p(HGNC:ANP32A) decreases act(p(FPLX:PPP2)) View Subject | View Object

Complementing these findings, immu- nohistochemical and western blot studies have shown re- duced expression of PPMT [77], and up-regulation of the PP2A inhibitors I 1 and I 2 in AD cases [79, 80]. PubMed:22299660

p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) negativeCorrelation act(p(FPLX:PPP2)) View Subject | View Object

Studies in transgenic mice and in cell cultures have shown a connection between PP2A loss of function and tau hyper-phosphorylation and aggregation into PHF. PubMed:22299660

p(HGNC:SET) decreases act(p(FPLX:PPP2)) View Subject | View Object

Complementing these findings, immu- nohistochemical and western blot studies have shown re- duced expression of PPMT [77], and up-regulation of the PP2A inhibitors I 1 and I 2 in AD cases [79, 80]. PubMed:22299660

path(MESH:"Alzheimer Disease") negativeCorrelation act(p(FPLX:PPP2)) View Subject | View Object

Several observations showing reduced PP2A activity by 30% in the frontal cortex in AD [55], were followed by a number of studies of PP2A mRNA and proteins. PubMed:22299660

Annotations
MeSH
Frontal Lobe

path(MESH:"Alzheimer Disease") negativeCorrelation act(p(FPLX:PPP2)) View Subject | View Object

To sum up, PP2A activity is decreased in brain of AD, as revealed by using different approaches in different laboratories. PubMed:22299660

Annotations
MeSH
Brain

path(MESH:"Down Syndrome") negativeCorrelation p(FPLX:PPP2) View Subject | View Object

Decreased of PP2A, but not of other phosphatases, has also been observed in Down syndrome correlating with increased tau pathology. PubMed:22299660

path(MESH:"Frontotemporal Dementia") association p(FPLX:PPP2) View Subject | View Object

So far, the most explored pathologies in which PP2A is implicated are cancer, and some viral and parasitic diseases [44]. More recently, PP2A has been investigated in FTLD linked to mutations in the tau gene [45]. PubMed:22299660

path(MESH:Neoplasms) association p(FPLX:PPP2) View Subject | View Object

So far, the most explored pathologies in which PP2A is implicated are cancer, and some viral and parasitic diseases [44]. More recently, PP2A has been investigated in FTLD linked to mutations in the tau gene [45]. PubMed:22299660

Out-Edges 58

act(p(FPLX:PPP2)) positiveCorrelation complex(p(FPLX:PPP2), p(HGNC:MAPT)) View Subject | View Object

Notably, methylation of PP2A catalytic C subunit on the Leu- 309 residue by leucine carboxyl methyltransferase 1 (LCMT1) promotes the biogenesis and stabilization of PP2A/B enzymes (20). We have shown that decreased LCMT1 activity and/or expression levels correlate with down-regulation of PP2A methylation and PP2A/B expression levels and with concomitant accumulation of phospho-Tau in AD-affected brain regions (21), in cultured N2a neuroblastoma cells and in vivo PubMed:23943618

Appears in Networks:
Annotations
Disease Ontology (DO)
Alzheimer's disease

act(p(FPLX:PPP2), ma(kin)) positiveCorrelation p(HGNC:UNC5B) View Subject | View Object

Overexpression of UNC5B induces neuronal death by activating death-associated protein kinase (DAPK1) (19) via protein phosphatase 2A-mediated dephosphorylation of DAPK1 (20). PubMed:27068745

Appears in Networks:

act(p(FPLX:PPP2), ma(kin)) increases act(p(HGNC:DAPK1)) View Subject | View Object

Overexpression of UNC5B induces neuronal death by activating death-associated protein kinase (DAPK1) (19) via protein phosphatase 2A-mediated dephosphorylation of DAPK1 (20). PubMed:27068745

Appears in Networks:

act(p(FPLX:PPP2)) association p(FPLX:PPP2, pmod(Ph)) View Subject | View Object

Methylation [52] and phosphorylation [53] are two major modifications that have been shown to modulate PP2A catalytic efficiency. PubMed:23454242

act(p(FPLX:PPP2)) association p(FPLX:PPP2, pmod(Me)) View Subject | View Object

Methylation [52] and phosphorylation [53] are two major modifications that have been shown to modulate PP2A catalytic efficiency. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"glycolytic process") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"lipid metabolic process") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"catecholamine biosynthetic process") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"cell cycle") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"DNA replication") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"transcription, DNA-templated") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

act(p(FPLX:PPP2)) decreases p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) View Subject | View Object

In Alzheimer's disease, inhibition of PP2A activity by SET leads to hyper phosphorylation of the Tau protein [47]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:translation) View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"signal transduction") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"cell population proliferation") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"cell population proliferation") View Subject | View Object

Co-immunoprecipitation and in-vitro pull down assay using pro-lymphoid FL5.12 cells showed a direct association of the PP2A-B55 holoenzyme with Akt, which selectively regulates phosphorylation of Akt at Thr-308 and regulates cell proliferation and survival [58]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"cytoskeleton organization") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) increases bp(GO:"cytoskeleton organization") View Subject | View Object

During meiosis I, Shugoshins binds to PP2A and dephosphorylates cohesion, which prevents spindle microtubules disassembly [37]. PP2APR55 also dephosphorylates vimentin (intermediate filament) and protects cytoskeleton disassembly [38]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"cell motility") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"apoptotic process") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) regulates bp(GO:"apoptotic process") View Subject | View Object

Co-immunoprecipitation and in-vitro pull down assay using pro-lymphoid FL5.12 cells showed a direct association of the PP2A-B55 holoenzyme with Akt, which selectively regulates phosphorylation of Akt at Thr-308 and regulates cell proliferation and survival [58]. PubMed:23454242

p(FPLX:PPP2) association path(MESH:"Cell Transformation, Neoplastic") View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) association path(MESH:Neoplasms) View Subject | View Object

PP2A is an important player in many cellular functions. It controls cell metabolism by regulating the activity of the enzymes involved in glycolysis, lipid metabolism and catecholamine synthesis [8]. It also regulates various biological processes such as the cell cycle (by mediating cdc2 kinase activation), DNA replication, transcription and translation, signal transduction, cell proliferation, cytoskeleton dynamics and cell mobility and apoptosis. It has also been shown to play a role in cell transformation and cancer [9-12]. PubMed:23454242

p(FPLX:PPP2) decreases path(MESH:Neoplasms) View Subject | View Object

PP2A is considered as a tumor suppressor and is thought to be functionally inactivated in cancer. PubMed:23454242

act(p(FPLX:PPP2)) negativeCorrelation path(MESH:Neoplasms) View Subject | View Object

PP2A is considered as a tumor suppressor and is thought to be functionally inactivated in cancer. PubMed:23454242

p(FPLX:PPP2) decreases p(HGNC:VIM, pmod(Ph)) View Subject | View Object

During meiosis I, Shugoshins binds to PP2A and dephosphorylates cohesion, which prevents spindle microtubules disassembly [37]. PP2APR55 also dephosphorylates vimentin (intermediate filament) and protects cytoskeleton disassembly [38]. PubMed:23454242

p(FPLX:PPP2) decreases p(FPLX:AKT, pmod(Ph, Thr, 308)) View Subject | View Object

Co-immunoprecipitation and in-vitro pull down assay using pro-lymphoid FL5.12 cells showed a direct association of the PP2A-B55 holoenzyme with Akt, which selectively regulates phosphorylation of Akt at Thr-308 and regulates cell proliferation and survival [58]. PubMed:23454242

p(FPLX:PPP2) decreases p(HGNC:CTNNB1, pmod(Ph)) View Subject | View Object

In Xenopus, PP2A- B56 is involved in β -catenin dephosphorylation and degradation and its phosphorylation directs activation of the Wnt pathway [43]. PubMed:23454242

p(FPLX:PPP2) increases deg(p(HGNC:CTNNB1)) View Subject | View Object

In Xenopus, PP2A- B56 is involved in β -catenin dephosphorylation and degradation and its phosphorylation directs activation of the Wnt pathway [43]. PubMed:23454242

p(FPLX:PPP2) decreases p(HGNC:BAD, pmod(Ph)) View Subject | View Object

Phosphorylation of BAD suppresses, and its dephosphorylation by PP2A promotes pro-apoptotic activity [59]. Additionally, phosphorylation of Bcl-2 activates, and its dephosphorylation by PP2A suppresses anti- apoptotic activity. PubMed:23454242

p(FPLX:PPP2) decreases p(HGNC:BCL2, pmod(Ph)) View Subject | View Object

Phosphorylation of BAD suppresses, and its dephosphorylation by PP2A promotes pro-apoptotic activity [59]. Additionally, phosphorylation of Bcl-2 activates, and its dephosphorylation by PP2A suppresses anti- apoptotic activity. PubMed:23454242

p(FPLX:PPP2) association path(MESH:"Frontotemporal Dementia") View Subject | View Object

So far, the most explored pathologies in which PP2A is implicated are cancer, and some viral and parasitic diseases [44]. More recently, PP2A has been investigated in FTLD linked to mutations in the tau gene [45]. PubMed:22299660

p(FPLX:PPP2) negativeCorrelation path(MESH:"Down Syndrome") View Subject | View Object

Decreased of PP2A, but not of other phosphatases, has also been observed in Down syndrome correlating with increased tau pathology. PubMed:22299660

p(FPLX:PPP2) decreases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

Tau protein is rapidly dephosphorylated by endogenous phosphatases such as protein phosphatases 1, 2A, and 2B (cal- cineurin) that are all present in the brain, and effec- tively dephosphorylate tau protein in vitro. PubMed:12428809

p(FPLX:PPP2) association a(MESH:Cytosol) View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

p(FPLX:PPP2) association a(MESH:"Cell Nucleus") View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

p(FPLX:PPP2) association a(MESH:Mitochondria) View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

p(FPLX:PPP2) association a(MESH:Cytoskeleton) View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

p(FPLX:PPP2) association a(MESH:"Cell Membrane") View Subject | View Object

PP2A is mainly pre- sent as a soluble protein in the cytosol but it is also encoun- tered in the nucleus, mitochondria, cytoskeleton, and mem- branes. PubMed:22299660

p(FPLX:PPP2) association path(MESH:Neoplasms) View Subject | View Object

So far, the most explored pathologies in which PP2A is implicated are cancer, and some viral and parasitic diseases [44]. More recently, PP2A has been investigated in FTLD linked to mutations in the tau gene [45]. PubMed:22299660

act(p(FPLX:PPP2)) negativeCorrelation p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) View Subject | View Object

Studies in transgenic mice and in cell cultures have shown a connection between PP2A loss of function and tau hyper-phosphorylation and aggregation into PHF. PubMed:22299660

act(p(FPLX:PPP2)) negativeCorrelation a(HBP:"paired helical filaments") View Subject | View Object

Studies in transgenic mice and in cell cultures have shown a connection between PP2A loss of function and tau hyper-phosphorylation and aggregation into PHF. PubMed:22299660

act(p(FPLX:PPP2)) decreases p(HGNC:MAPT, pmod(Ph, Ser, 202), pmod(Ph, Thr, 205)) View Subject | View Object

Trans- genic mice with reduced PP2A activity show increased tau phosphorylation at Ser202/Thr205 and Ser42 [46]. PubMed:22299660

act(p(FPLX:PPP2)) decreases p(HGNC:MAPT, pmod(Ph, Ser, 242)) View Subject | View Object

Trans- genic mice with reduced PP2A activity show increased tau phosphorylation at Ser202/Thr205 and Ser42 [46]. PubMed:22299660

act(p(FPLX:PPP2)) decreases act(p(HGNC:CDK5)) View Subject | View Object

Moreover, some tau kinases as cyclin- dependent kinase 5 (cdk5) and TPKI (thiamine pyrophos- phokinase 1)/GSK3 (glycogen synthase kinase 3) are acti- vated following PP2A inhibition in starved mice [51]. PubMed:22299660

act(p(FPLX:PPP2)) decreases act(p(HGNC:TPK1)) View Subject | View Object

Moreover, some tau kinases as cyclin- dependent kinase 5 (cdk5) and TPKI (thiamine pyrophos- phokinase 1)/GSK3 (glycogen synthase kinase 3) are acti- vated following PP2A inhibition in starved mice [51]. PubMed:22299660

act(p(FPLX:PPP2)) decreases act(p(HGNC:GSK3B)) View Subject | View Object

Moreover, some tau kinases as cyclin- dependent kinase 5 (cdk5) and TPKI (thiamine pyrophos- phokinase 1)/GSK3 (glycogen synthase kinase 3) are acti- vated following PP2A inhibition in starved mice [51]. PubMed:22299660

act(p(FPLX:PPP2)) negativeCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

Several observations showing reduced PP2A activity by 30% in the frontal cortex in AD [55], were followed by a number of studies of PP2A mRNA and proteins. PubMed:22299660

Annotations
MeSH
Frontal Lobe

act(p(FPLX:PPP2)) negativeCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

To sum up, PP2A activity is decreased in brain of AD, as revealed by using different approaches in different laboratories. PubMed:22299660

Annotations
MeSH
Brain

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BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.